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TPIS_BOVIN
ID   TPIS_BOVIN              Reviewed;         249 AA.
AC   Q5E956;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Triosephosphate isomerase;
DE            Short=TIM;
DE            EC=5.3.1.1 {ECO:0000255|PROSITE-ProRule:PRU10127};
DE   AltName: Full=Methylglyoxal synthase {ECO:0000250|UniProtKB:P00939};
DE            EC=4.2.3.3 {ECO:0000250|UniProtKB:P00939};
DE   AltName: Full=Triose-phosphate isomerase;
GN   Name=TPI1;
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].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Triosephosphate isomerase is an extremely efficient metabolic
CC       enzyme that catalyzes the interconversion between dihydroxyacetone
CC       phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis
CC       and gluconeogenesis. {ECO:0000250|UniProtKB:P00939}.
CC   -!- FUNCTION: It is also responsible for the non-negligible production of
CC       methylglyoxal a reactive cytotoxic side-product that modifies and can
CC       alter proteins, DNA and lipids. {ECO:0000250|UniProtKB:P00939}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dihydroxyacetone phosphate = methylglyoxal + phosphate;
CC         Xref=Rhea:RHEA:17937, ChEBI:CHEBI:17158, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57642; EC=4.2.3.3;
CC         Evidence={ECO:0000250|UniProtKB:P00939};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate;
CC         Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776;
CC         EC=5.3.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10127};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate from glycerone phosphate: step 1/1. {ECO:0000255|PROSITE-
CC       ProRule:PRU10127}.
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000255|PROSITE-ProRule:PRU10127}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|PROSITE-ProRule:PRU10127}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU10127}.
CC   -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; BT021064; AAX09081.1; -; mRNA.
DR   EMBL; BC102903; AAI02904.1; -; mRNA.
DR   RefSeq; NP_001013607.1; NM_001013589.3.
DR   AlphaFoldDB; Q5E956; -.
DR   SMR; Q5E956; -.
DR   IntAct; Q5E956; 1.
DR   STRING; 9913.ENSBTAP00000026358; -.
DR   Allergome; 11905; Bos d TPI.
DR   PaxDb; Q5E956; -.
DR   PeptideAtlas; Q5E956; -.
DR   PRIDE; Q5E956; -.
DR   GeneID; 281543; -.
DR   KEGG; bta:281543; -.
DR   CTD; 7167; -.
DR   eggNOG; KOG1643; Eukaryota.
DR   HOGENOM; CLU_024251_2_0_1; -.
DR   InParanoid; Q5E956; -.
DR   OrthoDB; 1272577at2759; -.
DR   TreeFam; TF300829; -.
DR   UniPathway; UPA00109; UER00189.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008929; F:methylglyoxal synthase activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0004807; F:triose-phosphate isomerase activity; ISS:UniProtKB.
DR   GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR   GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0019563; P:glycerol catabolic process; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR   GO; GO:0019242; P:methylglyoxal biosynthetic process; ISS:UniProtKB.
DR   CDD; cd00311; TIM; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00147_B; TIM_B; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR035990; TIM_sf.
DR   InterPro; IPR022896; TrioseP_Isoase_bac/euk.
DR   InterPro; IPR000652; Triosephosphate_isomerase.
DR   InterPro; IPR020861; Triosephosphate_isomerase_AS.
DR   PANTHER; PTHR21139; PTHR21139; 1.
DR   Pfam; PF00121; TIM; 1.
DR   SUPFAM; SSF51351; SSF51351; 1.
DR   TIGRFAMs; TIGR00419; tim; 1.
DR   PROSITE; PS00171; TIM_1; 1.
DR   PROSITE; PS51440; TIM_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase;
KW   Isopeptide bond; Lyase; Methylation; Nitration; Phosphoprotein;
KW   Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P60174"
FT   CHAIN           2..249
FT                   /note="Triosephosphate isomerase"
FT                   /id="PRO_0000236271"
FT   ACT_SITE        96
FT                   /note="Electrophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT   ACT_SITE        166
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT   BINDING         12
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT   BINDING         14
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT   MOD_RES         14
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P60174"
FT   MOD_RES         68
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P17751"
FT   MOD_RES         80
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P60174"
FT   MOD_RES         106
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48500"
FT   MOD_RES         149
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P17751"
FT   MOD_RES         156
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P17751"
FT   MOD_RES         156
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P17751"
FT   MOD_RES         159
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P17751"
FT   MOD_RES         173
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P17751"
FT   MOD_RES         194
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P60174"
FT   MOD_RES         194
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P60174"
FT   MOD_RES         194
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P17751"
FT   MOD_RES         198
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48500"
FT   MOD_RES         209
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P17751"
FT   MOD_RES         212
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P60174"
FT   MOD_RES         214
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P60174"
FT   MOD_RES         223
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P60174"
FT   MOD_RES         238
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P60174"
FT   CROSSLNK        142
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT                   /evidence="ECO:0000250|UniProtKB:P60174"
SQ   SEQUENCE   249 AA;  26690 MW;  8349A3A2AAC92D30 CRC64;
     MAPSRKFFVG GNWKMNGRKN NLGELINTLN AAKVPADTEV VCAPPTAYID FARQKLDPKI
     AVAAQNCYKV ANGAFTGEIS PGMIKDLGAT WVVLGHSERR HVFGESDELI GQKVAHALAE
     GLGVIACIGE KLDEREAGIT EKVVFEQTKV IADNVKDWSK VVLAYEPVWA IGTGKTATPQ
     QAQEVHEKLR GWLKSNVSDA VAQSARIIYG GSVTGATCKE LASQPDVDGF LVGGASLKPE
     FVDIINAKQ
 
 
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