TPIS_CHICK
ID TPIS_CHICK Reviewed; 248 AA.
AC P00940;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 168.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3885220; DOI=10.1073/pnas.82.7.2014;
RA Straus D., Gilbert W.;
RT "Chicken triosephosphate isomerase complements an Escherichia coli
RT deficiency.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:2014-2018(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3837846; DOI=10.1128/mcb.5.12.3497-3506.1985;
RA Straus D., Gilbert W.;
RT "Genetic engineering in the Precambrian: structure of the chicken
RT triosephosphate isomerase gene.";
RL Mol. Cell. Biol. 5:3497-3506(1985).
RN [3]
RP PROTEIN SEQUENCE OF 2-248.
RX PubMed=4463937; DOI=10.1042/bj1390011;
RA Furth A.J., Milman J.D., Priddle J.D., Offord R.E.;
RT "Studies on the subunit structure and amino acid sequence of trisoe
RT phosphate isomerase from chicken breast muscle.";
RL Biochem. J. 139:11-22(1974).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND SEQUENCE REVISION.
RX PubMed=1134550; DOI=10.1038/255609a0;
RA Banner D.W., Bloomer A.C., Petsko G.A., Phillips D.C., Pogson C.I.,
RA Wilson I.A., Corran P.H., Furth A.J., Milman J.D., Offord R.E.,
RA Priddle J.D., Waley S.G.;
RT "Structure of chicken muscle triose phosphate isomerase determined
RT crystallographically at 2.5-A resolution using amino acid sequence data.";
RL Nature 255:609-614(1975).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND MUTAGENESIS OF HIS-95 AND
RP GLU-165.
RX PubMed=2361134; DOI=10.1021/bi00469a012;
RA Blacklow S.C., Knowles J.R.;
RT "How can a catalytic lesion be offset? The energetics of two
RT pseudorevertant triosephosphate isomerases.";
RL Biochemistry 29:4099-4108(1990).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=985462; DOI=10.1016/0006-291x(76)90972-4;
RA Banner D.W., Bloomer A.C., Petsko G.A., Phillips D.C., Wilson I.A.;
RT "Atomic coordinates for triose phosphate isomerase from chicken muscle.";
RL Biochem. Biophys. Res. Commun. 72:146-155(1976).
RN [7]
RP COMPARISON OF X-RAY STRUCTURES.
RX PubMed=1569570; DOI=10.1016/0022-2836(92)90473-w;
RA Wierenga R.K., Noble M.E.M., Davenport R.C.;
RT "Comparison of the refined crystal structures of liganded and unliganded
RT chicken, yeast and trypanosomal triosephosphate isomerase.";
RL J. Mol. Biol. 224:1115-1126(1992).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT ASP-165 IN COMPLEX WITH
RP SUBSTRATE ANALOG, ACTIVE SITE, AND SUBSTRATE BINDING-SITE.
RX PubMed=8130195; DOI=10.1021/bi00176a012;
RA Zhang Z., Sugio S., Komives E.A., Liu K.D., Knowles J.R., Petsko G.A.,
RA Ringe D.;
RT "Crystal structure of recombinant chicken triosephosphate isomerase-
RT phosphoglycolohydroxamate complex at 1.8-A resolution.";
RL Biochemistry 33:2830-2837(1994).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RA Artymiuk P.J., Taylor W.R., Phillips D.C.;
RL Submitted (AUG-1998) to the PDB data bank.
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 ECO:0000269|PubMed:8130195}.
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; M11314; AAA49094.1; -; mRNA.
DR EMBL; M11941; AAA49095.1; -; Genomic_DNA.
DR PIR; A23448; ISCHT.
DR RefSeq; NP_990782.1; NM_205451.1.
DR PDB; 1SPQ; X-ray; 2.16 A; A/B=2-248.
DR PDB; 1SQ7; X-ray; 2.85 A; A/B=2-248.
DR PDB; 1SSD; X-ray; 2.90 A; A/B=2-248.
DR PDB; 1SSG; X-ray; 2.90 A; A/B=2-248.
DR PDB; 1SU5; X-ray; 2.70 A; A/B=2-248.
DR PDB; 1SW0; X-ray; 1.71 A; A/B=1-248.
DR PDB; 1SW3; X-ray; 2.03 A; A/B=1-248.
DR PDB; 1SW7; X-ray; 2.22 A; A/B=1-248.
DR PDB; 1TIM; X-ray; 2.50 A; A/B=2-248.
DR PDB; 1TPB; X-ray; 1.90 A; 1/2=2-248.
DR PDB; 1TPC; X-ray; 1.90 A; 1/2=2-248.
DR PDB; 1TPH; X-ray; 1.80 A; 1/2=2-248.
DR PDB; 1TPU; X-ray; 1.90 A; A/B=2-248.
DR PDB; 1TPV; X-ray; 1.90 A; A/B=2-248.
DR PDB; 1TPW; X-ray; 1.90 A; A/B=2-248.
DR PDB; 4P61; X-ray; 1.34 A; A/B=1-248.
DR PDB; 8TIM; X-ray; 2.50 A; A/B=2-248.
DR PDBsum; 1SPQ; -.
DR PDBsum; 1SQ7; -.
DR PDBsum; 1SSD; -.
DR PDBsum; 1SSG; -.
DR PDBsum; 1SU5; -.
DR PDBsum; 1SW0; -.
DR PDBsum; 1SW3; -.
DR PDBsum; 1SW7; -.
DR PDBsum; 1TIM; -.
DR PDBsum; 1TPB; -.
DR PDBsum; 1TPC; -.
DR PDBsum; 1TPH; -.
DR PDBsum; 1TPU; -.
DR PDBsum; 1TPV; -.
DR PDBsum; 1TPW; -.
DR PDBsum; 4P61; -.
DR PDBsum; 8TIM; -.
DR AlphaFoldDB; P00940; -.
DR BMRB; P00940; -.
DR SMR; P00940; -.
DR BioGRID; 676684; 1.
DR IntAct; P00940; 1.
DR STRING; 9031.ENSGALP00000023396; -.
DR PaxDb; P00940; -.
DR Ensembl; ENSGALT00000023442; ENSGALP00000023396; ENSGALG00000014526.
DR Ensembl; ENSGALT00000071768; ENSGALP00000044536; ENSGALG00000014526.
DR GeneID; 396435; -.
DR KEGG; gga:396435; -.
DR CTD; 7167; -.
DR VEuPathDB; HostDB:geneid_396435; -.
DR eggNOG; KOG1643; Eukaryota.
DR GeneTree; ENSGT00390000013354; -.
DR HOGENOM; CLU_024251_2_0_1; -.
DR InParanoid; P00940; -.
DR OMA; QEVCGAI; -.
DR OrthoDB; 1272577at2759; -.
DR PhylomeDB; P00940; -.
DR TreeFam; TF300829; -.
DR BRENDA; 5.3.1.1; 1306.
DR Reactome; R-GGA-352875; Gluconeogenesis.
DR Reactome; R-GGA-352882; Glycolysis.
DR Reactome; R-GGA-70171; Glycolysis.
DR Reactome; R-GGA-70263; Gluconeogenesis.
DR SABIO-RK; P00940; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; P00940; -.
DR PRO; PR:P00940; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000014526; Expressed in muscle tissue and 14 other tissues.
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:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0061621; P:canonical glycolysis; IEA:Ensembl.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Gluconeogenesis;
KW Glycolysis; Isomerase; Lyase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:4463937"
FT CHAIN 2..248
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090121"
FT ACT_SITE 95
FT /note="Electrophile"
FT /evidence="ECO:0000269|PubMed:8130195,
FT ECO:0007744|PDB:1TPH"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:8130195,
FT ECO:0007744|PDB:1TPH"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:8130195,
FT ECO:0007744|PDB:1TPH"
FT BINDING 13
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:8130195,
FT ECO:0007744|PDB:1TPH"
FT MUTAGEN 95
FT /note="H->N: Reduces activity 5000-fold."
FT /evidence="ECO:0000269|PubMed:2361134"
FT MUTAGEN 165
FT /note="E->D: Reduces activity 300-fold."
FT /evidence="ECO:0000269|PubMed:2361134"
FT CONFLICT 17..18
FT /note="DK -> KR (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="N -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 145..146
FT /note="EQ -> QE (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="S -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 202..204
FT /note="QST -> VQS (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:4P61"
FT HELIX 18..30
FT /evidence="ECO:0007829|PDB:4P61"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:4P61"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:4P61"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:4P61"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:4P61"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:4P61"
FT HELIX 80..85
FT /evidence="ECO:0007829|PDB:4P61"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:4P61"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:4P61"
FT HELIX 106..118
FT /evidence="ECO:0007829|PDB:4P61"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:4P61"
FT HELIX 131..136
FT /evidence="ECO:0007829|PDB:4P61"
FT HELIX 139..151
FT /evidence="ECO:0007829|PDB:4P61"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:4P61"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:4P61"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:1SW0"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:1SW0"
FT HELIX 178..195
FT /evidence="ECO:0007829|PDB:4P61"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:4P61"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:4P61"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:4P61"
FT HELIX 217..221
FT /evidence="ECO:0007829|PDB:4P61"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:4P61"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:4P61"
FT HELIX 240..244
FT /evidence="ECO:0007829|PDB:4P61"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:4P61"
SQ SEQUENCE 248 AA; 26620 MW; AFCC258E574DE982 CRC64;
MAPRKFFVGG NWKMNGDKKS LGELIHTLNG AKLSADTEVV CGAPSIYLDF ARQKLDAKIG
VAAQNCYKVP KGAFTGEISP AMIKDIGAAW VILGHSERRH VFGESDELIG QKVAHALAEG
LGVIACIGEK LDEREAGITE KVVFEQTKAI ADNVKDWSKV VLAYEPVWAI GTGKTATPQQ
AQEVHEKLRG WLKSHVSDAV AQSTRIIYGG SVTGGNCKEL ASQHDVDGFL VGGASLKPEF
VDIINAKH
