ID A0A0C1VE90_9CYAN Unreviewed; 241 AA. AC A0A0C1VE90; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 22-FEB-2023, entry version 40. 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=QQ91_002245 {ECO:0000313|EMBL:NEV65931.1}; OS Lyngbya confervoides BDU141951. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Oscillatoriaceae; Lyngbya. OX NCBI_TaxID=1574623 {ECO:0000313|EMBL:NEV65931.1, ECO:0000313|Proteomes:UP000031561}; RN [1] {ECO:0000313|EMBL:NEV65931.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BDU141951 {ECO:0000313|EMBL:NEV65931.1}; RA Malar M.C., Sen D., Tripathy S.; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:NEV65931.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BDU141951 {ECO:0000313|EMBL:NEV65931.1}; RX PubMed=25745003; RA Chandrababunaidu M.M., Sen D., Tripathy S.; RT "Draft Genome Sequence of Filamentous Marine Cyanobacterium Lyngbya RT confervoides Strain BDU141951."; RL Genome Announc. 3:e00066-e00015(2015). RN [3] {ECO:0000313|EMBL:NEV65931.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BDU141951 {ECO:0000313|EMBL:NEV65931.1}; RA Sarangi A.N., Ghosh S., Mukherjee M., Tripathy S.; RL Submitted (FEB-2020) 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: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:NEV65931.1}. 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; JTHE02000002; NEV65931.1; -; Genomic_DNA. DR RefSeq; WP_039724861.1; NZ_JTHE02000002.1. DR AlphaFoldDB; A0A0C1VE90; -. DR EnsemblBacteria; KIF42492; KIF42492; QQ91_12995. DR UniPathway; UPA00109; UER00189. DR UniPathway; UPA00138; -. DR Proteomes; UP000031561; Unassembled WGS sequence. 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; Aldolase class I; 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; TRIOSEPHOSPHATE ISOMERASE; 1. DR PANTHER; PTHR21139:SF2; TRIOSEPHOSPHATE ISOMERASE; 1. DR Pfam; PF00121; TIM; 1. DR SUPFAM; SSF51351; Triosephosphate isomerase (TIM); 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}. FT ACT_SITE 96 FT /note="Electrophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00147" FT ACT_SITE 165 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00147" FT BINDING 9..11 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00147" FT BINDING 171 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00147" FT BINDING 204 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00147" FT BINDING 225..226 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00147" SQ SEQUENCE 241 AA; 26143 MW; E779D716F4DBF3CA CRC64; MRKIVIAGNW KMHKTQGDAL AFLQEFLNYL TETPDDREAV LCVPFTALGT LSKNLHGSLI KLGAQNIHWA DEGAFTGEIS GDMLSELGVR YVIVGHSERR QYFGETDETV NQRLLAAQRH GLTPILCVGE TKEQRDAGET DSIIAAQISK DLVDVDQSNL VIAYEPIWAI GTGDTCEATD ANKVIGAIRA QLTNQDVPIQ YGGSVKPGNI DEIMAQSEID GVLVGGASLQ AEGFARIVNF Q //