ID TPIS_BORAP Reviewed; 253 AA. AC Q0SPB0; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 16-JUN-2009, entry version 23. DE RecName: Full=Triosephosphate isomerase; DE Short=TIM; DE EC=5.3.1.1; DE AltName: Full=Triose-phosphate isomerase; GN Name=tpiA; OrderedLocusNames=BAPKO_0055; OS Borrelia afzelii (strain PKo). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia; OC Borrelia burgdorferi group. OX NCBI_TaxID=390236; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16914037; DOI=10.1186/1471-2164-7-211; RA Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., RA Suehnel J., Wilske B., Platzer M.; RT "Comparative genome analysis: selection pressure on the Borrelia vls RT cassettes is essential for infectivity."; RL BMC Genomics 7:211-211(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; CP000395; ABH01318.1; -; Genomic_DNA. DR RefSeq; YP_709494.1; -. DR GeneID; 4227598; -. DR GenomeReviews; CP000395_GR; BAPKO_0055. DR KEGG; baf:BAPKO_0055; -. DR NMPDR; fig|390236.5.peg.120; -. DR HOGENOM; Q0SPB0; -. DR OMA; Q0SPB0; IGAQDCH. DR BioCyc; BAFZ390236:BAPKO_0055-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 1 253 Triosephosphate isomerase. FT /FTId=PRO_0000307438. FT ACT_SITE 96 96 Electrophile (By similarity). FT ACT_SITE 169 169 Proton acceptor (By similarity). FT BINDING 9 9 Substrate (By similarity). FT BINDING 11 11 Substrate (By similarity). SQ SEQUENCE 253 AA; 27830 MW; EF737C12ACFCE32B CRC64; MRKTFLAGNW KMHYTSAEAS IVAKQIATEV KTLNDDFVIM ITPPFTALSK VSECIKGSNI LLGAQNMSYM ESGARTSEIS PSMLLEFGVE YVILGHSECR LYLAETDEII NKKIRAGLKH SFKYLILCVG ETLDERDSGK TLDVVLSQVK KGLDCVSESD IKRIILAYEP VWAIGTGKTA TKEEAEEVHK AIRLEIMKLY SKSASDNIII QYGGSVNASN IKELMNEPNI DGALIGGASL KAESFLSIIN NVR //