ID TPIS_ALHEH Reviewed; 250 AA. AC Q0A773; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 16-JUN-2009, entry version 21. DE RecName: Full=Triosephosphate isomerase; DE Short=TIM; DE EC=5.3.1.1; DE AltName: Full=Triose-phosphate isomerase; GN Name=tpiA; OrderedLocusNames=Mlg_1972; OS Alkalilimnicola ehrlichei (strain MLHE-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Alkalilimnicola. OX NCBI_TaxID=187272; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., RA King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., RA Xie G., Stolz J.F., Richardson P.; RT "Complete sequence of Alkalilimnicola ehrilichei MLHE-1."; RL Submitted (AUG-2006) 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; CP000453; ABI57314.1; -; Genomic_DNA. DR RefSeq; YP_742804.1; -. DR GeneID; 4268515; -. DR GenomeReviews; CP000453_GR; Mlg_1972. DR KEGG; aeh:Mlg_1972; -. DR NMPDR; fig|187272.6.peg.1879; -. DR HOGENOM; Q0A773; -. DR OMA; Q0A773; IGAQDCH. 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 1 250 Triosephosphate isomerase. FT /FTId=PRO_0000307422. FT ACT_SITE 94 94 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 250 AA; 26220 MW; 75DFB29834414F59 CRC64; MRKPMVAGNW KMNGSLALVN DMGRALADVD CSAVDVLVCP PFPYIGPLRR AVPDESGVAL GGQDVSRYDS GAYTGEVAGA MLAEMGCRHV IVGHSERRAM HAETDEVVVD KVQAALRAGL TPIVCVGETL EARDAGETEQ VVGRQLDAVL ELGGFVVEKL VLAYEPVWAI GTGRTASPEQ AQAVHAFIRQ RAADALGDEL AQRLPILYGG SVKPGNAREL FGCADVDGGL IGGASLDPDG FLEIISAARP //