ID   G6PI1_RHOJR             Reviewed;         550 AA.
AC   Q0S539;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Glucose-6-phosphate isomerase 1 {ECO:0000255|HAMAP-Rule:MF_00473};
DE            Short=GPI 1 {ECO:0000255|HAMAP-Rule:MF_00473};
DE            EC=5.3.1.9 {ECO:0000255|HAMAP-Rule:MF_00473};
DE   AltName: Full=Phosphoglucose isomerase 1 {ECO:0000255|HAMAP-Rule:MF_00473};
DE            Short=PGI 1 {ECO:0000255|HAMAP-Rule:MF_00473};
DE   AltName: Full=Phosphohexose isomerase 1 {ECO:0000255|HAMAP-Rule:MF_00473};
DE            Short=PHI 1 {ECO:0000255|HAMAP-Rule:MF_00473};
GN   Name=pgi1 {ECO:0000255|HAMAP-Rule:MF_00473};
GN   OrderedLocusNames=RHA1_ro05567;
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1;
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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}.
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DR   EMBL; CP000431; ABG97347.1; -; Genomic_DNA.
DR   RefSeq; WP_011597733.1; NC_008268.1.
DR   AlphaFoldDB; Q0S539; -.
DR   SMR; Q0S539; -.
DR   STRING; 101510.RHA1_ro05567; -.
DR   EnsemblBacteria; ABG97347; ABG97347; RHA1_ro05567.
DR   KEGG; rha:RHA1_ro05567; -.
DR   PATRIC; fig|101510.16.peg.5611; -.
DR   eggNOG; COG0166; Bacteria.
DR   HOGENOM; CLU_017947_3_1_11; -.
DR   OMA; IGVWYIN; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000008710; 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; 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; Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT   CHAIN           1..550
FT                   /note="Glucose-6-phosphate isomerase 1"
FT                   /id="PRO_0000252637"
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        512
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   550 AA;  60028 MW;  20C5F1651E86995C CRC64;
     MSSDITGTAA WQKLRDHHAQ IQSVHLRELF EKDPARGQEL TVTAGDLYID YSKHRIDRDT
     LGLLLELARS ADLEARRDAM FAGEHINTSE DRAVLHTALR LPADASLVVD GQDVVADVHE
     VLDRMGDFTD RVRSGEWRGA TGERIKTVVN IGIGGSDLGP VMVYRALRHY ADAGISVRFI
     SNVDPADLVR SLQGLDPATT LFIVASKTFS TLETLTNATA ARRWLLGGLG LGNEAVAKHF
     VAVSTHADRV AEFGIDTANM FGFWDWVGGR YSVDSAIGLS VMAAIGKERF AEFLAGFHAV
     DEHFRTAPLE ENAPVLLGLI GLWYSNFFGA ESRAVLPYSN DLVRFAAYLQ QLTMESNGKS
     VRADGTPVPT STGEIFWGEP GTNGQHAFYQ LLHQGTRLVP SDFIGFGEPT DDLPTADGTG
     SMHDLLMSNF FAQTKVLAFG KTAEEIAAEG TPEHLVPHKV MPGNRPSTTI LAPKLTPSVI
     GQLIALYEHQ VFVEGVVWGI DSFDQWGVEL GKTQAVELQP VLTAAEEPAA QSDSSTDSLV
     RWYRRQRGRA