ID A0A1I9XV56_9BURK Unreviewed; 238 AA. AC A0A1I9XV56; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 07-APR-2021, entry version 20. DE RecName: Full=Triosephosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013}; DE Short=TIM {ECO:0000256|HAMAP-Rule:MF_00147}; DE Short=TPI {ECO:0000256|HAMAP-Rule:MF_00147}; DE EC=5.3.1.1 {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013}; DE AltName: Full=Triose-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00147}; GN Name=tpiA {ECO:0000256|HAMAP-Rule:MF_00147}; GN ORFNames=YQ44_07130 {ECO:0000313|EMBL:APA67648.1}; OS Janthinobacterium sp. 1_2014MBL_MicDiv. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Janthinobacterium. OX NCBI_TaxID=1644131 {ECO:0000313|EMBL:APA67648.1, ECO:0000313|Proteomes:UP000180140}; RN [1] {ECO:0000313|EMBL:APA67648.1, ECO:0000313|Proteomes:UP000180140} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1_2014MBL_MicDiv {ECO:0000313|EMBL:APA67648.1, RC ECO:0000313|Proteomes:UP000180140}; RA Roller B., Bhatnagar S., Boitano M., Korlach J., Newman D.K., RA Leadbetter J.R., Dawson S.C.; RT "The Complete Genome Sequence of Janthinobacterium sp. str. RT 1_2014MBL_MicDiv."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes stereospecifically CC the conversion of dihydroxyacetone phosphate (DHAP) to D- CC glyceraldehyde-3-phosphate (G3P). {ECO:0000256|HAMAP-Rule:MF_00147}. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate; CC Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; CC EC=5.3.1.1; Evidence={ECO:0000256|HAMAP-Rule:MF_00147, CC ECO:0000256|RuleBase:RU363013}; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate from glycerone phosphate: step 1/1. {ECO:0000256|HAMAP- CC Rule:MF_00147, ECO:0000256|RuleBase:RU363013}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00147, CC ECO:0000256|RuleBase:RU363013}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00147, CC ECO:0000256|RuleBase:RU363013}. CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family. CC {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00147}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP011319; APA67648.1; -; Genomic_DNA. DR EnsemblBacteria; APA67648; APA67648; YQ44_07130. DR KEGG; jaz:YQ44_07130; -. DR UniPathway; UPA00109; UER00189. DR UniPathway; UPA00138; -. DR Proteomes; UP000180140; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule. DR CDD; cd00311; TIM; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00147_B; TIM_B; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR035990; TIM_sf. DR InterPro; IPR022896; TrioseP_Isoase_bac/euk. DR InterPro; IPR000652; Triosephosphate_isomerase. DR InterPro; IPR020861; Triosephosphate_isomerase_AS. DR PANTHER; PTHR21139; PTHR21139; 1. DR Pfam; PF00121; TIM; 1. DR SUPFAM; SSF51351; SSF51351; 1. DR TIGRFAMs; TIGR00419; tim; 1. DR PROSITE; PS00171; TIM_1; 1. DR PROSITE; PS51440; TIM_2; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013}; KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432, ECO:0000256|HAMAP- KW Rule:MF_00147}; KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_00147, KW ECO:0000256|RuleBase:RU363013}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00147}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..27 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 28..238 FT /note="Triosephosphate isomerase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5009606497" FT REGION 221..222 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00147" FT ACT_SITE 83 FT /note="Electrophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00147" FT ACT_SITE 155 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00147" FT BINDING 161 FT /note="Substrate; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00147" FT BINDING 200 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00147" SQ SEQUENCE 238 AA; 23865 MW; 13ACFA282A01F652 CRC64; MNGSRTSNAV LLSEIVAGLA ASGAASAVCV PAPYLAQCQA QLAGSALAWG GQDVSAHAGG AYTGEISTAM LQDFGCSYVV IGHSERRAYH GESDAQVAAK TVAALAAGIT PIVCIGETLA QREAGQTDAV VAQQLGAVLA AIGADDVARL VLAYEPVWAI GTGKTATPQM AQDVHLVLRG QLAEKNAVAA AGVQILYGGS MKPENAKELM AMPDIDGGLI GGAALKAADF LAIIHAAD //