ID TPIS2_RHIEC Reviewed; 267 AA. AC Q2JZQ2; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 16-JUN-2009, entry version 24. DE RecName: Full=Triosephosphate isomerase 2; DE Short=TIM 2; DE EC=5.3.1.1; DE AltName: Full=Triose-phosphate isomerase 2; GN Name=tpiA2; Synonyms=tpiAf; OrderedLocusNames=RHE_PF00040; OS Rhizobium etli (strain CFN 42 / ATCC 51251). OG Plasmid p42f. 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; CP000138; ABC93934.1; -; Genomic_DNA. DR RefSeq; YP_472661.1; -. DR GeneID; 3896224; -. DR GenomeReviews; CP000138_GR; RHE_PF00040. DR KEGG; ret:RHE_PF00040; -. DR HOGENOM; Q2JZQ2; -. DR OMA; Q2JZQ2; EHFGETD. 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; Plasmid. FT CHAIN 1 267 Triosephosphate isomerase 2. FT /FTId=PRO_0000236166. FT ACT_SITE 95 95 Electrophile (By similarity). FT ACT_SITE 168 168 Proton acceptor (By similarity). FT BINDING 10 10 Substrate (By similarity). SQ SEQUENCE 267 AA; 29175 MW; 3A6085823E800D93 CRC64; MVVWVGTSFK MNKTLEEALA FARRLADADL ERDPRVQRFV IPSFTAVREV KRVLTESSVK VGAQNMHWED AGAWTGEISP LMLKDCRLDL VELGHSERRE HFGETDETVG LKAAAAIRHG LTPLICIGET LQERNEGRAD AVLRRQVEAA LRGVDTEAGE APILLAYEPV WAIGVNGIPA TADYASERHR GIAEVAKSIL GRPVPVLYGG SVNPGNCEEL IGQPDIDGLF IGRSAWSVEG YLDILARVSA AIDRSSPRQT ASERKLP //