PGAM4_PANTR
ID PGAM4_PANTR Reviewed; 254 AA.
AC Q8MKE8; Q2VIN5;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Probable phosphoglycerate mutase 4;
DE EC=5.4.2.11 {ECO:0000250|UniProtKB:P18669};
DE EC=5.4.2.4 {ECO:0000250|UniProtKB:P18669};
GN Name=PGAM4; Synonyms=PGAM3;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11961099; DOI=10.1093/oxfordjournals.molbev.a004124;
RA Betran E., Wang W., Jin L., Long M.;
RT "Evolution of the phosphoglycerate mutase processed gene in human and
RT chimpanzee revealing the origin of a new primate gene.";
RL Mol. Biol. Evol. 19:654-663(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16201836; DOI=10.1371/journal.pbio.0030357;
RA Marques A.C., Dupanloup I., Vinckenbosch N., Reymond A., Kaessmann H.;
RT "Emergence of young human genes after a burst of retroposition in
RT primates.";
RL PLoS Biol. 3:E357-E357(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.11; Evidence={ECO:0000250|UniProtKB:P18669};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phospho-glyceroyl phosphate = (2R)-2,3-
CC bisphosphoglycerate + H(+); Xref=Rhea:RHEA:17765, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58248; EC=5.4.2.4;
CC Evidence={ECO:0000250|UniProtKB:P18669};
CC -!- MISCELLANEOUS: This is the product of a processed gene created by
CC retroposition from mRNA of an expressed gene. This gene seems to be
CC expressed.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000305}.
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DR EMBL; AF465746; AAM27297.1; -; Genomic_DNA.
DR EMBL; DQ120648; ABB92433.1; -; Genomic_DNA.
DR RefSeq; NP_001009163.1; NM_001009163.1.
DR AlphaFoldDB; Q8MKE8; -.
DR SMR; Q8MKE8; -.
DR STRING; 9598.ENSPTRP00000004915; -.
DR PaxDb; Q8MKE8; -.
DR PRIDE; Q8MKE8; -.
DR GeneID; 494122; -.
DR KEGG; ptr:494122; -.
DR CTD; 441531; -.
DR eggNOG; KOG0235; Eukaryota.
DR InParanoid; Q8MKE8; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0004082; F:bisphosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0004619; F:phosphoglycerate mutase activity; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR HAMAP; MF_01039; PGAM_GpmA; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR InterPro; IPR005952; Phosphogly_mut1.
DR PANTHER; PTHR11931; PTHR11931; 1.
DR Pfam; PF00300; His_Phos_1; 2.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR TIGRFAMs; TIGR01258; pgm_1; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 3: Inferred from homology;
KW Acetylation; Glycolysis; Hydrolase; Isomerase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..254
FT /note="Probable phosphoglycerate mutase 4"
FT /id="PRO_0000179833"
FT ACT_SITE 11
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT ACT_SITE 89
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT BINDING 10..17
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 23..24
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 89..92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 116..117
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 187..188
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT SITE 186
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT MOD_RES 26
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT MOD_RES 106
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBJ1"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBJ1"
FT MOD_RES 251
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT MOD_RES 251
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBJ1"
FT MOD_RES 253
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT MOD_RES 254
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P18669"
SQ SEQUENCE 254 AA; 28809 MW; 0F073CDE449EDD39 CRC64;
MAAYKLVLIR HGESTWNLEN RFSCWYDADL SPAGHEEAKR GGQALRDAGY EFDICLTSVQ
KRVIRTLWTV LDAIDQMWLP VVRTWRLNER HYGGLTALNK AETAAKHGEA QVKIWRRSYD
VPPPPMEPDH PFYSNISKDR RYADLTEDQL PSYESPKDTI ARALPFWNEE IVPQIKEGKR
VLIAAHGNSL QGIAKHVEGL SEEAIMELNL PTGIPIVYEL DKNLKPIKPM QFLGDEETVC
KAMEAVAAQG KAKK
