ID G6PI_SERP5 Reviewed; 548 AA. AC A8GKD1; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 1. DT 27-MAR-2024, entry version 84. 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=Spro_4477; OS Serratia proteamaculans (strain 568). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Serratia. OX NCBI_TaxID=399741; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=568; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L., RA Vangronsveld J., van der Lelie D., Richardson P.; RT "Complete sequence of chromosome of Serratia proteamaculans 568."; RL Submitted (SEP-2007) 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; CP000826; ABV43571.1; -; Genomic_DNA. DR AlphaFoldDB; A8GKD1; -. DR SMR; A8GKD1; -. DR STRING; 399741.Spro_4477; -. DR KEGG; spe:Spro_4477; -. DR eggNOG; COG0166; Bacteria. DR HOGENOM; CLU_017947_3_1_6; -. DR OrthoDB; 140919at2; -. DR UniPathway; UPA00109; UER00181. DR UniPathway; UPA00138; -. 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. FT CHAIN 1..548 FT /note="Glucose-6-phosphate isomerase" FT /id="PRO_1000060399" FT ACT_SITE 355 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473" FT ACT_SITE 386 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473" FT ACT_SITE 514 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473" SQ SEQUENCE 548 AA; 61018 MW; 3F8950438FF64D2E CRC64; MKNINPSQTA AWQALQQHFE QMKDVQISDL FAQDKERFSK FSATFNDQML VDYSKNRISA ETLEKLQALA KETDLQSAIK SMFAGEKINR TEDRAVLHVA LRNRSNTPII VDGKDVMPEV NAVLAKMKQF CDRVIGGDWK GYTGKAITDV VNIGIGGSDL GPYMATEALR PYKNHLNMHF VSNVDGTHIA ETLQPLNPET TLFLVASKTF TTQETMTNAH SARDWFLSTA GDQKHVAKHF AALSTNGKAV GGFGIDTANM FEFWDWVGGR YSLWSAIGLS IALSLGFDNF EQLLSGAHAM DQHFAQTPAE KNLPVLLALI GIWYNNFFGA ETEAILPYDQ YMHRFAAYFQ QGNMESNGKY VDRNGNPVDY QTGPIIWGEP GTNGQHAFYQ LIHQGTKLVP CDFIAPAISH NPLSDHHAKL LSNFFAQTEA LAFGKSLEVV EAEFAAQGKT PEEVKHVAPF KVFEGNRPTN SILLREITPF SLGSLIALYE HKIFTQGAIL NIFTFDQWGV ELGKQLANRI LPELAGDEAV SSHDSSTNAL INRFKEWR //