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PGAM2_BOVIN
ID   PGAM2_BOVIN             Reviewed;         253 AA.
AC   Q32KV0;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Phosphoglycerate mutase 2;
DE            EC=5.4.2.11 {ECO:0000250|UniProtKB:P18669};
DE            EC=5.4.2.4 {ECO:0000250|UniProtKB:P18669};
DE   AltName: Full=BPG-dependent PGAM 2;
GN   Name=PGAM2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Interconversion of 3- and 2-phosphoglycerate with 2,3-
CC       bisphosphoglycerate as the primer of the reaction. Can also catalyze
CC       the reaction of EC 5.4.2.4 (synthase), but with a reduced activity.
CC       {ECO:0000250}.
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC       dependent PGAM subfamily. {ECO:0000305}.
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DR   EMBL; BC109918; AAI09919.1; -; mRNA.
DR   RefSeq; NP_001033200.1; NM_001038111.2.
DR   AlphaFoldDB; Q32KV0; -.
DR   SMR; Q32KV0; -.
DR   STRING; 9913.ENSBTAP00000019336; -.
DR   PaxDb; Q32KV0; -.
DR   PeptideAtlas; Q32KV0; -.
DR   PRIDE; Q32KV0; -.
DR   GeneID; 515067; -.
DR   KEGG; bta:515067; -.
DR   CTD; 5224; -.
DR   eggNOG; KOG0235; Eukaryota.
DR   InParanoid; Q32KV0; -.
DR   OrthoDB; 804949at2759; -.
DR   Proteomes; UP000009136; 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   2: Evidence at transcript level;
KW   Glycolysis; Hydrolase; Isomerase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..253
FT                   /note="Phosphoglycerate mutase 2"
FT                   /id="PRO_0000282827"
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         3
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P16290"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P16290"
FT   MOD_RES         118
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O70250"
FT   MOD_RES         132
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P16290"
FT   MOD_RES         133
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P16290"
FT   MOD_RES         135
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P16290"
FT   MOD_RES         152
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P16290"
SQ   SEQUENCE   253 AA;  28685 MW;  13DF4728D4D9D17D CRC64;
     MSTHRLVMVR HGESTWNQEN RFCGWFDAEL SEKGAEEAKK AAQAIKDAKM EFDICYTSVL
     KRAIRTLWTI LDGTDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEE QVKIWRRSFD
     IPPPPMDEKH PYYKSISKER RYAGLKAGEL PTCESLKDTI ARALPFWNDE IAPQIKAGKR
     VLIAAHGNSL RGIVKHLEGM SDQAIMELNL PTGIPIVYEL DQALKPTKPM RFLGDEETVR
     KAMEAVAAQG KAK
 
 
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