ID A0A090IWM7_9BACI Unreviewed; 451 AA. AC A0A090IWM7; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 22-JUL-2015, entry version 8. DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00473, ECO:0000256|RuleBase:RU000612}; DE Short=GPI {ECO:0000256|HAMAP-Rule:MF_00473}; DE EC=5.3.1.9 {ECO:0000256|HAMAP-Rule:MF_00473, ECO:0000256|RuleBase:RU000612}; DE AltName: Full=Phosphoglucose isomerase {ECO:0000256|HAMAP-Rule:MF_00473}; DE AltName: Full=Phosphohexose isomerase {ECO:0000256|HAMAP-Rule:MF_00473}; GN Name=pgiA {ECO:0000313|EMBL:CEE02491.1}; GN Synonyms=pgi {ECO:0000256|HAMAP-Rule:MF_00473}; GN ORFNames=B4064_0919 {ECO:0000313|EMBL:KIO67298.1}, B4065_1086 GN {ECO:0000313|EMBL:KIO65142.1}, B4166_2159 GN {ECO:0000313|EMBL:KIO68383.1}, B4167_2242 GN {ECO:0000313|EMBL:KIO73269.1}, BT1A1_2698 GN {ECO:0000313|EMBL:CEE02491.1}; OS Bacillus thermoamylovorans. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=35841 {ECO:0000313|EMBL:CEE02491.1}; RN [1] {ECO:0000313|EMBL:CEE02491.1} RP NUCLEOTIDE SEQUENCE. RA Wibberg Daniel; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KIO65142.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=B4064 {ECO:0000313|EMBL:KIO67298.1}, B4065 RC {ECO:0000313|EMBL:KIO65142.1}, B4166 {ECO:0000313|EMBL:KIO68383.1}, RC and B4167 {ECO:0000313|EMBL:KIO73269.1}; RA Krawcyk A.O., Berendsen E.M., Eijlander R.T., de Jong A., RA Wells-Bennik M., Kuipers O.P.; RT "Draft Genome Sequences of Four Bacillus thermoamylovorans Strains, RT Isolated From Food Products."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate = D-fructose 6- CC phosphate. {ECO:0000256|HAMAP-Rule:MF_00473, CC ECO:0000256|RuleBase:RU000612, ECO:0000256|SAAS:SAAS00031303}. 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|HAMAP-Rule:MF_00473, ECO:0000256|RuleBase:RU000612, CC ECO:0000256|SAAS:SAAS00031250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00473, CC ECO:0000256|SAAS:SAAS00031298}. CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|HAMAP- CC Rule:MF_00473, ECO:0000256|RuleBase:RU000612}. 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; CCRF01000077; CEE02491.1; -; Genomic_DNA. DR EMBL; JXLS01000059; KIO65142.1; -; Genomic_DNA. DR EMBL; JXLR01000035; KIO67298.1; -; Genomic_DNA. DR EMBL; JXLT01000041; KIO68383.1; -; Genomic_DNA. DR EMBL; JXLU01000051; KIO73269.1; -; Genomic_DNA. DR RefSeq; WP_034772024.1; NZ_JXLU01000051.1. DR EnsemblBacteria; CEE02491; CEE02491; BT1A1_2698. DR UniPathway; UPA00109; UER00181. DR UniPathway; UPA00138; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004347; F:glucose-6-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 HAMAP; MF_00473; G6P_isomerase; 1. DR InterPro; IPR001672; G6P_Isomerase. DR InterPro; IPR018189; Phosphoglucose_isomerase_CS. DR PANTHER; PTHR11469; PTHR11469; 1. DR Pfam; PF00342; PGI; 1. DR PRINTS; PR00662; G6PISOMERASE. 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 ECO:0000256|SAAS:SAAS00031240}; KW Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_00473, KW ECO:0000256|RuleBase:RU000612}; KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_00473, KW ECO:0000256|RuleBase:RU000612}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00473, KW ECO:0000256|RuleBase:RU000612}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00473}. FT ACT_SITE 426 426 {ECO:0000256|HAMAP-Rule:MF_00473}. FT MOD_RES 38 38 Phosphothreonine. {ECO:0000256|HAMAP- FT Rule:MF_00473}. SQ SEQUENCE 451 AA; 50380 MW; 38F5FBC805CF8438 CRC64; MTHIQFDYSK ALSFFKPHEL TQMKDLVKVS HHALHEGTGA GNDFRGWIDL PVNYDKEEFA RILKAAEKIK NDSDVLIVIG IGGSYLGARA AIEMLNHSFY NAMPKEKRGG TPQVIFAGNN ISSSYLTDVI DLLEGKDWSI NVISKSGTTT EPAIAFRIFR KLLQEKYGVD EARKRIYATT DRARGALKTL ATEEGYETFV VPDDIGGRYS VLTAVGLLPI AVSGVNIEEM MKGAAKARED FASSELEENL AYQYAAVRNI LYNKGKTIEM LINYEPGLQY FAEWWKQLFG ESEGKDQKGI YPSSANFSTD LHSLGQYVQE GRRDIFETVI KVDKPRHELV IEAEDNDLDG LNYLAGKTVD FVNTKAFEGT ILAHTDGNVP NLVVTIPQMD AYTFGYLVYF FEKACAISGY LLGVNPFDQP GVEAYKVNMF ALLGKPGFEE KKAELEKRLQ S //