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 16-JUN-2009, entry version 24. DE RecName: Full=Triosephosphate isomerase A; DE Short=TIM-A; DE EC=5.3.1.1; 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 Cyprinidae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=21518599; PubMed=11606544; RA Merritt T.J.S., Quattro J.M.; RT "Evidence for a period of directional selection following gene RT duplication in a neurally expressed locus of triosephosphate RT isomerase."; RL Genetics 159:689-697(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen; RG The Danio rerio sequencing project at the Sanger Institute; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. 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 -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate = glycerone CC phosphate. CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate from glycerone phosphate: step 1/1. CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF387820; AAK85203.1; -; mRNA. DR EMBL; AL772314; CAK11229.1; -; Genomic_DNA. DR EMBL; BC049500; AAH49500.1; -; mRNA. DR IPI; IPI00498329; -. DR RefSeq; NP_705953.1; -. DR UniGene; Dr.82679; -. DR SMR; Q1MTI4; 4-247. DR Ensembl; ENSDARG00000025012; Danio rerio. DR GeneID; 192309; -. DR KEGG; dre:192309; -. DR NMPDR; fig|7955.3.peg.9678; -. DR ZFIN; ZDB-GENE-020416-3; tpi1a. DR HOVERGEN; Q1MTI4; -. DR OMA; Q1MTI4; PNCIFLY. DR ArrayExpress; Q1MTI4; -. DR Bgee; Q1MTI4; -. DR GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:EC. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW. DR GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-KW. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000652; Triosephosphate_isomerase. DR Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1. DR PANTHER; PTHR21139; Triophos_ismrse; 1. DR Pfam; PF00121; TIM; 1. DR ProDom; PD001005; Triophos_ismrse; 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 Fatty acid biosynthesis; Gluconeogenesis; Glycolysis; Isomerase; KW Lipid synthesis; Pentose shunt. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 248 Triosephosphate isomerase A. FT /FTId=PRO_0000345140. FT ACT_SITE 95 95 Electrophile (By similarity). FT ACT_SITE 165 165 Proton acceptor (By similarity). FT BINDING 11 11 Substrate (By similarity). FT BINDING 13 13 Substrate (By similarity). FT CONFLICT 36 36 E -> K (in Ref. 1; AAK85203). FT CONFLICT 134 134 R -> K (in Ref. 2; AAH49500). FT CONFLICT 179 179 E -> G (in Ref. 2; AAH49500). FT CONFLICT 190 190 G -> E (in Ref. 1; AAK85203). 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 //