ID A0A4Z0LL28_9RHOB Unreviewed; 533 AA. AC A0A4Z0LL28; DT 18-SEP-2019, integrated into UniProtKB/TrEMBL. DT 18-SEP-2019, sequence version 1. DT 25-MAY-2022, entry version 10. 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=EYC08_07920 {ECO:0000313|EMBL:TGD65011.1}; OS Tabrizicola sp. WMC-M-20. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Tabrizicola; unclassified Tabrizicola. OX NCBI_TaxID=2528693 {ECO:0000313|EMBL:TGD65011.1, ECO:0000313|Proteomes:UP000298307}; RN [1] {ECO:0000313|EMBL:TGD65011.1, ECO:0000313|Proteomes:UP000298307} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WMC-M-20 {ECO:0000313|EMBL:TGD65011.1, RC ECO:0000313|Proteomes:UP000298307}; RA Liu Z., Li A., Zhou Y.; RL Submitted (FEB-2019) 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: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:TGD65011.1}. 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; SJDN01000004; TGD65011.1; -; Genomic_DNA. DR UniPathway; UPA00109; UER00181. DR UniPathway; UPA00138; -. DR Proteomes; UP000298307; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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; PTHR11469; 1. DR Pfam; PF00342; PGI; 1. DR PRINTS; PR00662; G6PISOMERASE. DR SUPFAM; SSF53697; SSF53697; 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}. FT ACT_SITE 341 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473" FT ACT_SITE 372 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473" FT ACT_SITE 501 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473" SQ SEQUENCE 533 AA; 57619 MW; 85A8B689B139DAB6 CRC64; MNQHWDALKD HHAAVEGRPI LDLFEDGTRA AEFTARADGM ILDFAKTNID ARGRALLLQL AEAAGVADKR AAMFAGAKIN ETEGRAVLHT ALRNMDTPLM VDGQDVTIAL RETHARMTAF ADDVRTGRFT GQGGKITDVV NIGIGGSDLG PAMAVLALAP FHNGPRVHFI SNVDGAHAAD TLQGLNPETT LVIVASKTFT TIETMTNAET VRVWMAQKVA NPAAQFAAVS TAAQKTSAFG IASERVFGFE DWVGGRYSMW GPIGLSLMLA MGPEGFAAFL RGGAAMDAHF RTAPFAENLP VLLALVGIWH NQICGYTTRA VLPYDQRLSR LPAYLQQLEM ESNGKRVAMD GTDLPYHSGP VVWGEPGTNG QHAFYQLIHQ GTRVVPCEFL VARRGHEPDL AHQHLLLVSN CLAQSEALLR GRSLAEATAI MAKKGLTGAE LDRQARHRVF PGNRPSTTLA YDQLTPFVLG QIIALYEHRV FVEGVILGIN SYDQWGVELG KELALALQPM LEGKADTAGK DGSTRQLVDW ARG //