ID A0A0C1VE90_9CYAN Unreviewed; 241 AA. AC A0A0C1VE90; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 12-APR-2017, entry version 18. 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_12995 {ECO:0000313|EMBL:KIF42492.1}; OS Lyngbya confervoides BDU141951. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Oscillatoriaceae; Lyngbya. OX NCBI_TaxID=1574623 {ECO:0000313|EMBL:KIF42492.1, ECO:0000313|Proteomes:UP000031561}; RN [1] {ECO:0000313|EMBL:KIF42492.1, ECO:0000313|Proteomes:UP000031561} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BDU141951 {ECO:0000313|EMBL:KIF42492.1, RC ECO:0000313|Proteomes:UP000031561}; RA Malar M.C., Sen D., Tripathy S.; RT "Draft genome sequence of Lyngbya confervoides BDU141951."; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes CC stereospecifically the conversion of dihydroxyacetone phosphate CC (DHAP) to D-glyceraldehyde-3-phosphate (G3P). {ECO:0000256|HAMAP- CC Rule:MF_00147}. CC -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate = glycerone CC phosphate. {ECO:0000256|HAMAP-Rule:MF_00147, CC ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00728719}. CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013, CC ECO:0000256|SAAS:SAAS00728615}. 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 ECO:0000256|SAAS:SAAS00728661}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00147, CC ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00728692}. 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 ECO:0000256|SAAS:SAAS00728708}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIF42492.1}. 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; JTHE01000261; KIF42492.1; -; Genomic_DNA. DR RefSeq; WP_039724861.1; NZ_JTHE01000261.1. 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-HAMAP. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-HAMAP. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-HAMAP. 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; 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 Complete proteome {ECO:0000313|Proteomes:UP000031561}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00147, KW ECO:0000256|RuleBase:RU363013}; KW Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_00147, KW ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00728593}; KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_00147, KW ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00728672}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00147, KW ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00498630, KW ECO:0000313|EMBL:KIF42492.1}; KW Pentose shunt {ECO:0000256|HAMAP-Rule:MF_00147, KW ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00728639}; KW Reference proteome {ECO:0000313|Proteomes:UP000031561}. FT REGION 9 11 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00147}. FT REGION 225 226 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00147}. FT ACT_SITE 96 96 Electrophile. {ECO:0000256|HAMAP-Rule: FT MF_00147}. FT ACT_SITE 165 165 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_00147}. FT BINDING 171 171 Substrate; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00147}. FT BINDING 204 204 Substrate. {ECO:0000256|HAMAP-Rule: FT 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 //