ID A0A090IWM7_9BACI Unreviewed; 451 AA. AC A0A090IWM7; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 29-MAY-2024, entry version 50. 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=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}, BT1A1_2698 GN {ECO:0000313|EMBL:CEE02491.1}, CQJ30_14725 GN {ECO:0000313|EMBL:AWI13285.1}; OS Caldibacillus thermoamylovorans. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Caldibacillus. OX NCBI_TaxID=35841 {ECO:0000313|EMBL:CEE02491.1, ECO:0000313|Proteomes:UP000040576}; RN [1] {ECO:0000313|EMBL:CEE02491.1, ECO:0000313|Proteomes:UP000040576} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Wibberg Daniel; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000032071, ECO:0000313|Proteomes:UP000032078} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B4064 {ECO:0000313|EMBL:KIO67298.1, RC ECO:0000313|Proteomes:UP000032078}, and B4065 RC {ECO:0000313|EMBL:KIO65142.1, ECO:0000313|Proteomes:UP000032071}; RA Krawcyk A.O., Berendsen E.M., Eijlander R.T., de Jong A., Wells-Bennik M., RA 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. RN [3] {ECO:0000313|EMBL:AWI13285.1, ECO:0000313|Proteomes:UP000244914} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SSBM {ECO:0000313|EMBL:AWI13285.1, RC ECO:0000313|Proteomes:UP000244914}; RX PubMed=29625286; DOI=10.1016/j.biortech.2018.03.121; RA Cai L., Zheng S.W., Shen Y.J., Zheng G.D., Liu H.T., Wu Z.Y.; RT "Complete genome sequence provides insights into the biodrying-related RT microbial function of Bacillus thermoamylovorans isolated from sewage RT sludge biodrying material."; RL Bioresour. Technol. 260:141-149(2018). 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; CP023704; AWI13285.1; -; Genomic_DNA. DR EMBL; CCRF01000077; CEE02491.1; -; Genomic_DNA. DR EMBL; JXLS01000059; KIO65142.1; -; Genomic_DNA. DR EMBL; JXLR01000035; KIO67298.1; -; Genomic_DNA. DR RefSeq; WP_034772024.1; NZ_JXLU01000051.1. DR STRING; 35841.B4167_2242; -. DR KEGG; bthv:CQJ30_14725; -. DR PATRIC; fig|35841.6.peg.3738; -. DR eggNOG; COG0166; Bacteria. DR OrthoDB; 140919at2; -. DR UniPathway; UPA00109; UER00181. DR UniPathway; UPA00138; -. DR Proteomes; UP000032071; Unassembled WGS sequence. DR Proteomes; UP000032078; Unassembled WGS sequence. DR Proteomes; UP000040576; Unassembled WGS sequence. DR Proteomes; UP000244914; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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:0048029; F:monosaccharide binding; IEA:TreeGrafter. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule. DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IEA:TreeGrafter. 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; 2. 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:UP000040576}. FT ACT_SITE 291 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473" FT ACT_SITE 426 FT /evidence="ECO:0000256|HAMAP-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 //