GenomeNet

Database: UniProt
Entry: A0A3B4BPV8_PYGNA
LinkDB: A0A3B4BPV8_PYGNA
Original site: A0A3B4BPV8_PYGNA 
ID   A0A3B4BPV8_PYGNA        Unreviewed;       254 AA.
AC   A0A3B4BPV8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Phosphoglycerate mutase {ECO:0000256|RuleBase:RU004511};
DE            EC=5.4.2.11 {ECO:0000256|RuleBase:RU004511};
DE            EC=5.4.2.4 {ECO:0000256|RuleBase:RU004511};
OS   Pygocentrus nattereri (Red-bellied piranha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Pygocentrus.
OX   NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000000620.1, ECO:0000313|Proteomes:UP000261440};
RN   [1] {ECO:0000313|Ensembl:ENSPNAP00000000620.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00036552};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15903;
CC         Evidence={ECO:0000256|ARBA:ARBA00036552};
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:0000256|ARBA:ARBA00000505,
CC         ECO:0000256|RuleBase:RU004511};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC       dependent PGAM subfamily. {ECO:0000256|ARBA:ARBA00006717,
CC       ECO:0000256|RuleBase:RU004511}.
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   RefSeq; XP_017579660.1; XM_017724171.1.
DR   AlphaFoldDB; A0A3B4BPV8; -.
DR   STRING; 42514.ENSPNAP00000000620; -.
DR   Ensembl; ENSPNAT00000013545.1; ENSPNAP00000000620.1; ENSPNAG00000007625.1.
DR   GeneID; 108443463; -.
DR   CTD; 323107; -.
DR   GeneTree; ENSGT00950000182926; -.
DR   OMA; RMLPYWY; -.
DR   OrthoDB; 1008469at2759; -.
DR   Proteomes; UP000261440; Unplaced.
DR   GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004082; F:bisphosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 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   NCBIfam; TIGR01258; pgm_1; 1.
DR   PANTHER; PTHR11931; PHOSPHOGLYCERATE MUTASE; 1.
DR   PANTHER; PTHR11931:SF15; PHOSPHOGLYCERATE MUTASE 1; 1.
DR   Pfam; PF00300; His_Phos_1; 2.
DR   PIRSF; PIRSF000709; 6PFK_2-Ptase; 2.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU004511};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU004511}.
FT   ACT_SITE        11
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        89
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         10..17
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         89..92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         116..117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         187..188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   SITE            186
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-3"
SQ   SEQUENCE   254 AA;  29006 MW;  79AC0EEA2A7E6CEB CRC64;
     MAAYKLVLIR HGESCWNQEN RFCGWFDADL SETGRQEANR GGQALKDAGF EFDICYTSVL
     KRAIRTLWIV LDGIDQMWLP VHRTWRLNER HYGGLTGLNK AETAAKHGEA QVKIWRRSYD
     IPPPPMEADH DYYSVISKDR RYADLTEDQL PSCESLKDTI ARALPFWNEE IVPQIKKGKR
     VLIAAHGNSL RGIVKHLEGM SEEEIMELNL PTGIPILYEL DKNLKPIKPM QFLGDEETVR
     KAMEAVAAQG KAKK
//
DBGET integrated database retrieval system