ID A0A1H5SQ85_9CLOT Unreviewed; 450 AA. AC A0A1H5SQ85; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 03-MAY-2023, entry version 22. DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00473}; DE Short=GPI {ECO:0000256|HAMAP-Rule:MF_00473}; DE EC=5.3.1.9 {ECO:0000256|HAMAP-Rule:MF_00473}; DE AltName: Full=Phosphoglucose isomerase {ECO:0000256|HAMAP-Rule:MF_00473}; DE Short=PGI {ECO:0000256|HAMAP-Rule:MF_00473}; DE AltName: Full=Phosphohexose isomerase {ECO:0000256|HAMAP-Rule:MF_00473}; DE Short=PHI {ECO:0000256|HAMAP-Rule:MF_00473}; GN Name=pgi {ECO:0000256|HAMAP-Rule:MF_00473}; GN ORFNames=SAMN05660865_00428 {ECO:0000313|EMBL:SEF52128.1}; OS Caloramator fervidus. OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Caloramator. OX NCBI_TaxID=29344 {ECO:0000313|EMBL:SEF52128.1, ECO:0000313|Proteomes:UP000242850}; RN [1] {ECO:0000313|Proteomes:UP000242850} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5463 {ECO:0000313|Proteomes:UP000242850}; RA Varghese N., Submissions S.; RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate CC to fructose-6-phosphate. {ECO:0000256|HAMAP-Rule:MF_00473}. CC -!- CATALYTIC ACTIVITY: CC Reaction=alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate; CC Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57634, ChEBI:CHEBI:58225; CC EC=5.3.1.9; Evidence={ECO:0000256|ARBA:ARBA00029321, CC ECO:0000256|HAMAP-Rule:MF_00473, ECO:0000256|RuleBase:RU000612}; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000256|HAMAP-Rule:MF_00473}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 2/4. CC {ECO:0000256|ARBA:ARBA00004926, ECO:0000256|HAMAP-Rule:MF_00473, CC ECO:0000256|RuleBase:RU000612}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00473}. CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|ARBA:ARBA00006604, CC ECO:0000256|HAMAP-Rule:MF_00473, ECO:0000256|RuleBase:RU000612}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00473}. 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; FNUK01000003; SEF52128.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1H5SQ85; -. DR EnsemblBacteria; SEF52128; SEF52128; SAMN05660865_00428. DR OrthoDB; 140919at2; -. DR UniPathway; UPA00109; UER00181. DR UniPathway; UPA00138; -. DR Proteomes; UP000242850; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro. DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-UniRule. DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule. DR CDD; cd05015; SIS_PGI_1; 1. DR CDD; cd05016; SIS_PGI_2; 1. DR HAMAP; MF_00473; G6P_isomerase; 1. DR InterPro; IPR001672; G6P_Isomerase. DR InterPro; IPR018189; Phosphoglucose_isomerase_CS. DR InterPro; IPR046348; SIS_dom_sf. DR InterPro; IPR035476; SIS_PGI_1. DR InterPro; IPR035482; SIS_PGI_2. DR PANTHER; PTHR11469; GLUCOSE-6-PHOSPHATE ISOMERASE; 1. DR PANTHER; PTHR11469:SF1; GLUCOSE-6-PHOSPHATE ISOMERASE; 1. DR Pfam; PF00342; PGI; 1. DR PRINTS; PR00662; G6PISOMERASE. DR SUPFAM; SSF53697; SIS domain; 1. DR PROSITE; PS00765; P_GLUCOSE_ISOMERASE_1; 1. DR PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1. DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00473}; KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432, ECO:0000256|HAMAP- KW Rule:MF_00473}; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP- KW Rule:MF_00473}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00473}; KW Reference proteome {ECO:0000313|Proteomes:UP000242850}. FT ACT_SITE 290 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473" FT ACT_SITE 425 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473" SQ SEQUENCE 450 AA; 50977 MW; 8C7B11362230AF45 CRC64; MKNITLDYSK VLPFVKVEEI NNLESQIKDA HEKLHNKTGP GSDFLGWVTL PRDYDKDEFK RILRAAERIK ENSDVFVVIG IGGSYLGARA AIEMLNHTFY NILPKNKRKT PEIYFVGNNI SPVYMHDLLE ILEGKDISVN VISKSGTTTE PAIAFRILKE YMERKYGKEE ARKRIYATTD KSKGALRKLA EEEGYETFVI PDDVGGRYSV LTAVGLLPIA VSGVDIKEII KGAQDGMDEY SNLDVFNNAA YLYAAIRNIL YRKGKTVEIM ANYEPGLHYF AEWWKQLFGE SEGKDGKGIY PASVDFTTDL HSMGQYIQDG LRHIFETVLN VEKPRYDIEI MEDKDNIDGL NFLAGKTMDF VNKKAFEGTV LAHTDGNVPN IIINIPELTP YYFGKLVYMF EKACGISGYI LGVNPFDQPG VEAYKKNMFA LLGKPGFEEQ RRKLEEILGR //