TPISB_DANRE
ID TPISB_DANRE Reviewed; 248 AA.
AC Q90XG0; Q7T315;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Triosephosphate isomerase B;
DE Short=TIM-B;
DE EC=5.3.1.1 {ECO:0000255|PROSITE-ProRule:PRU10127};
DE AltName: Full=Methylglyoxal synthase B {ECO:0000250|UniProtKB:P00939};
DE EC=4.2.3.3 {ECO:0000250|UniProtKB:P00939};
DE AltName: Full=Triose-phosphate isomerase B;
GN Name=tpi1b;
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 MRNA].
RC TISSUE=Embryo, and Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-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; AF387819; AAK85202.1; -; mRNA.
DR EMBL; BC152271; AAI52272.1; -; mRNA.
DR EMBL; BC053294; AAH53294.1; -; mRNA.
DR RefSeq; NP_705954.2; NM_153668.4.
DR AlphaFoldDB; Q90XG0; -.
DR SMR; Q90XG0; -.
DR STRING; 7955.ENSDARP00000060055; -.
DR PaxDb; Q90XG0; -.
DR PRIDE; Q90XG0; -.
DR GeneID; 560753; -.
DR KEGG; dre:560753; -.
DR CTD; 560753; -.
DR ZFIN; ZDB-GENE-020416-4; tpi1b.
DR eggNOG; KOG1643; Eukaryota.
DR InParanoid; Q90XG0; -.
DR OrthoDB; 1272577at2759; -.
DR PhylomeDB; Q90XG0; -.
DR TreeFam; TF300829; -.
DR Reactome; R-DRE-70171; Glycolysis.
DR Reactome; R-DRE-70263; Gluconeogenesis.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR PRO; PR:Q90XG0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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 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 B"
FT /id="PRO_0000345141"
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 56
FT /note="D -> N (in Ref. 2; AAH53294/AAI52272)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 26828 MW; CFD29D9A6E7918C8 CRC64;
MSGRKFFVGG NWKMNGDKKS IEELANTLNS AKLNPDTEVV CGAPTIYLDY ARSKLDPNID
VAAQNCYKVA KGAFTGEISP AMIKDCGVKW VILGHSERRH VFGESDELIG QKVAHALENG
LGVIACIGEK LDEREAGITE KVVFAQTKFI ADNVKDWSKV VLAYEPVWAI GTGKTASPQQ
AQEVHDKLRQ WLKTNVSEAV ANSVRIIYGG SVTGGTCKEL ASQKDLDGFL VGGASLKPEF
IDIINAKA
