TPISA_DANRE
ID TPISA_DANRE Reviewed; 248 AA.
AC Q1MTI4; Q7ZWB0; Q90XF9;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Triosephosphate isomerase A;
DE Short=TIM-A;
DE EC=5.3.1.1 {ECO:0000255|PROSITE-ProRule:PRU10127};
DE AltName: Full=Methylglyoxal synthase A {ECO:0000250|UniProtKB:P00939};
DE EC=4.2.3.3 {ECO:0000250|UniProtKB:P00939};
DE AltName: Full=Triose-phosphate isomerase A;
GN Name=tpi1a; ORFNames=si:dkey-89b17.2;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11606544; DOI=10.1093/genetics/159.2.689;
RA Merritt T.J.S., Quattro J.M.;
RT "Evidence for a period of directional selection following gene duplication
RT in a neurally expressed locus of triosephosphate isomerase.";
RL Genetics 159:689-697(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2003) 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; AF387820; AAK85203.1; -; mRNA.
DR EMBL; AL772314; CAK11229.1; -; Genomic_DNA.
DR EMBL; BC049500; AAH49500.1; -; mRNA.
DR RefSeq; NP_705953.1; NM_153667.2.
DR AlphaFoldDB; Q1MTI4; -.
DR SMR; Q1MTI4; -.
DR STRING; 7955.ENSDARP00000033907; -.
DR PaxDb; Q1MTI4; -.
DR PRIDE; Q1MTI4; -.
DR Ensembl; ENSDART00000037007; ENSDARP00000033907; ENSDARG00000025012.
DR GeneID; 192309; -.
DR KEGG; dre:192309; -.
DR CTD; 192309; -.
DR ZFIN; ZDB-GENE-020416-3; tpi1a.
DR eggNOG; KOG1643; Eukaryota.
DR GeneTree; ENSGT00390000013354; -.
DR HOGENOM; CLU_024251_2_0_1; -.
DR InParanoid; Q1MTI4; -.
DR OMA; VWAIGEH; -.
DR OrthoDB; 1272577at2759; -.
DR PhylomeDB; Q1MTI4; -.
DR TreeFam; TF300829; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR PRO; PR:Q1MTI4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 19.
DR Bgee; ENSDARG00000025012; Expressed in testis and 25 other tissues.
DR ExpressionAtlas; Q1MTI4; baseline and differential.
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 Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Lyase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..248
FT /note="Triosephosphate isomerase A"
FT /id="PRO_0000345140"
FT ACT_SITE 95
FT /note="Electrophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT BINDING 13
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT CONFLICT 36
FT /note="E -> K (in Ref. 1; AAK85203)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="R -> K (in Ref. 2; AAH49500)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="E -> G (in Ref. 2; AAH49500)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="G -> E (in Ref. 1; AAK85203)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 26853 MW; 546B461C6CBD1610 CRC64;
MSSRKFFVGG NWKMNGDKES LGELIMTLNT ASLNDETDVV CGAPSIYLDY ARSKLDQRIG
VAAQNCYKVP KGAFTGEISP AMIKDCGIDW VILGHSERRH VFGESDELIG QKVAHCLESD
LGVIACIGEK LEEREAGTTE DVVFEQTKVI ADNVKDWTRV VLAYEPVWAI GTGKTASPEQ
AQEVHEKLRG WLRANVSDAV ADSVRIIYGG SVTGGNCKEL AAQADVDGFL VGGASLKPEF
VDIINARS
