ID TPIS_ANAVT Reviewed; 241 AA. AC Q3M7Y8; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2005, sequence version 1. DT 16-JUN-2009, entry version 25. DE RecName: Full=Triosephosphate isomerase; DE Short=TIM; DE EC=5.3.1.1; DE AltName: Full=Triose-phosphate isomerase; GN Name=tpiA; OrderedLocusNames=Ava_3290; OS Anabaena variabilis (strain ATCC 29413 / PCC 7937). OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena. OX NCBI_TaxID=240292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., RA Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.; RT "Complete sequence of Anabaena variabilis ATCC 29413."; RL Submitted (SEP-2005) 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 -!- 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; CP000117; ABA22898.1; -; Genomic_DNA. DR RefSeq; YP_323793.1; -. DR GeneID; 3680321; -. DR GenomeReviews; CP000117_GR; Ava_3290. DR KEGG; ava:Ava_3290; -. DR NMPDR; fig|240292.3.peg.2096; -. DR HOGENOM; Q3M7Y8; -. DR OMA; Q3M7Y8; IGAQDCH. DR BioCyc; AVAR240292:AVA_3290-MON; -. 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 1 241 Triosephosphate isomerase. FT /FTId=PRO_0000307423. FT ACT_SITE 96 96 Electrophile (By similarity). FT ACT_SITE 165 165 Proton acceptor (By similarity). FT BINDING 9 9 Substrate (By similarity). FT BINDING 11 11 Substrate (By similarity). SQ SEQUENCE 241 AA; 26577 MW; 10BDF34603CF661D CRC64; MRKIVIAGNW KMFKTQAESQ EFLKEFLPAL EETPQEREVL LCVPFTDLAI LSQSLHGSLV QLGAQNVHWA ENGAYTGEIS GPMLTEIGVR YVIVGHSERR QFFGETDETV NLRLQAAQKY GLTPILCVGE TKQQRDSGET ESLIVSQLDK DLINVDQTNL VIAYEPIWAI GTGDTCETTE ANRVIGLIRS QLKNPDVPIQ YGGSVKPNNI DEIMAQPEID GVLVGGASLE AASFARIVNY Q //