ID TPIS1_RHIEC Reviewed; 256 AA. AC Q2K869; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 2. DT 16-JUN-2009, entry version 25. DE RecName: Full=Triosephosphate isomerase 1; DE Short=TIM 1; DE EC=5.3.1.1; DE AltName: Full=Triose-phosphate isomerase 1; GN Name=tpiA; Synonyms=tpiAch; OrderedLocusNames=RHE_CH02186; OS Rhizobium etli (strain CFN 42 / ATCC 51251). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=347834; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16505379; DOI=10.1073/pnas.0508502103; RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I., RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A., RA Jimenez-Jacinto V., Collado-Vides J., Davila G.; RT "The partitioned Rhizobium etli genome: genetic and metabolic RT redundancy in seven interacting replicons."; RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006). 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 -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable). 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; CP000133; ABC90967.1; ALT_INIT; Genomic_DNA. DR RefSeq; YP_469694.1; -. DR GeneID; 3892228; -. DR GenomeReviews; CP000133_GR; RHE_CH02186. DR KEGG; ret:RHE_CH02186; -. DR HOGENOM; Q2K869; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:HAMAP. DR GO; GO:0006094; P:gluconeogenesis; IEA:HAMAP. DR GO; GO:0006096; P:glycolysis; IEA:HAMAP. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:HAMAP. DR HAMAP; MF_00147; -; 1. 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 3: Inferred from homology; KW Complete proteome; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; KW Pentose shunt. FT CHAIN 1 256 Triosephosphate isomerase 1. FT /FTId=PRO_0000236165. FT ACT_SITE 99 99 Electrophile (By similarity). FT ACT_SITE 169 169 Proton acceptor (By similarity). FT BINDING 12 12 Substrate (By similarity). FT BINDING 14 14 Substrate (By similarity). SQ SEQUENCE 256 AA; 26953 MW; 795C601B8262CCAE CRC64; MTPDVRPLVA GNWKMNGTRA SLDQIKAIAE GVRPPLADKV EALICPPTTL LYVATALCTD SPLAIGAQDC HQKPSGAHTG DISAEMIADS FGTYVIVGHS ERRTDHAETD HLVRAKAEAA FAAELTAIIC IGETADERRA GQELDVIKRQ LSASVPDAAT AENTVIAYEP IWAIGTGVTP TSGDVEKAHA FMRAELVSRF GDEGRKMRLL YGGSVKPANA GELLGIANVD GALIGGASLK AADFLAIYRA YEALLA //