ID G6PI_LEPCP Reviewed; 545 AA. AC B1Y2Y7; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 1. DT 27-MAR-2024, entry version 85. DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00473}; DE Short=GPI {ECO:0000255|HAMAP-Rule:MF_00473}; DE EC=5.3.1.9 {ECO:0000255|HAMAP-Rule:MF_00473}; DE AltName: Full=Phosphoglucose isomerase {ECO:0000255|HAMAP-Rule:MF_00473}; DE Short=PGI {ECO:0000255|HAMAP-Rule:MF_00473}; DE AltName: Full=Phosphohexose isomerase {ECO:0000255|HAMAP-Rule:MF_00473}; DE Short=PHI {ECO:0000255|HAMAP-Rule:MF_00473}; GN Name=pgi {ECO:0000255|HAMAP-Rule:MF_00473}; GN OrderedLocusNames=Lcho_3385; OS Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix OS discophora (strain SP-6)). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Sphaerotilaceae; Leptothrix. OX NCBI_TaxID=395495; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51168 / LMG 8142 / SP-6; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Lykidis A., Emerson D., Richardson P.; RT "Complete sequence of Leptothrix cholodnii SP-6."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate CC to fructose-6-phosphate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00473}; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_00473}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00473}. CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000255|HAMAP- CC 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; CP001013; ACB35643.1; -; Genomic_DNA. DR RefSeq; WP_012348390.1; NC_010524.1. DR AlphaFoldDB; B1Y2Y7; -. DR SMR; B1Y2Y7; -. DR STRING; 395495.Lcho_3385; -. DR KEGG; lch:Lcho_3385; -. DR eggNOG; COG0166; Bacteria. DR HOGENOM; CLU_017947_3_1_4; -. DR OrthoDB; 140919at2; -. DR UniPathway; UPA00109; UER00181. DR UniPathway; UPA00138; -. DR Proteomes; UP000001693; Chromosome. 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: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 Gene3D; 1.10.1390.10; -; 1. DR HAMAP; MF_00473; G6P_isomerase; 1. DR InterPro; IPR001672; G6P_Isomerase. DR InterPro; IPR023096; G6P_Isomerase_C. 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; Gluconeogenesis; Glycolysis; Isomerase; Reference proteome. FT CHAIN 1..545 FT /note="Glucose-6-phosphate isomerase" FT /id="PRO_1000125738" FT ACT_SITE 345 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473" FT ACT_SITE 376 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473" FT ACT_SITE 514 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473" SQ SEQUENCE 545 AA; 58306 MW; B78C22550CD49E22 CRC64; MNTPRCDQTA AWAALAAHHQ GAGRQFDLRT AFGADAGRFD AFSLQAPEVF ADLSKNHWDA TTRGLLLGLA RQCQIESRRD AMLAGEPINH TEGRAVLHTA LRAPRGAAPF SDDVHGVLDA MLAYVEQVRD TATSGIKHVV NIGIGGSDLG PQMVVPALDA YAQRGLQLHF VSNVDGHDIA PVLRDLNPRE TLVIVASKTF TTQETMANAQ VARTWFLAGY GEGGEAAIAK HFAASTTNVA AAAKFGITTT FGFWDWVGGR YSLWSAIGLP IALAVGAENF RALLAGAHAM DRHFATAPLE SNLPIQLGLL DVWYRNFLGY TSRSIAPYHQ GLRRLPAYLQ QLEMESNGKC VDLDGASLPY GTCPVVWGEA GTNGQHAYFQ MLHQGTDVIP VEFIAVKTPN HGPDVADELK AGLADQHVKL LANCLAQSQA LMLGKTTDDA LTDKAPTAST ALDALTVARH RTFPGNRPSS TLVLDRLSPA SLGALIALYE HRVYTSGALW GINSFDQWGV ELGKALCNQL LPRFASGESA GLDASTAGLL ARLRG //