ID   G6PI1_THIDA             Reviewed;         550 AA.
AC   Q3SK65;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
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}; OrderedLocusNames=Tbd_0974;
OS   Thiobacillus denitrificans (strain ATCC 25259).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=292415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25259;
RX   PubMed=16452431; DOI=10.1128/jb.188.4.1473-1488.2006;
RA   Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA   Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT   "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT   anaerobic bacterium Thiobacillus denitrificans.";
RL   J. Bacteriol. 188:1473-1488(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; CP000116; AAZ96927.1; -; Genomic_DNA.
DR   RefSeq; WP_011311486.1; NC_007404.1.
DR   AlphaFoldDB; Q3SK65; -.
DR   SMR; Q3SK65; -.
DR   STRING; 292415.Tbd_0974; -.
DR   EnsemblBacteria; AAZ96927; AAZ96927; Tbd_0974.
DR   KEGG; tbd:Tbd_0974; -.
DR   eggNOG; COG0166; Bacteria.
DR   HOGENOM; CLU_017947_3_1_4; -.
DR   OMA; CPAYAYG; -.
DR   OrthoDB; 417261at2; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000008291; 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_0000230939"
FT   ACT_SITE        353
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        384
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        512
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   550 AA;  61247 MW;  46D040BDA2F8EEBF CRC64;
     MKPLKTLPAW KALEQHFKSM RNFDMRAAFR EDAARFETLS LRCGNLLLDY SKNRVTQETM
     RHLAQLARES ELEEMRNAMC TGERINFTEK RAVLHVALRA PVRPALMVEG VDVEREIAKV
     LHRMQRFVES VHNGSWRGHT GKPIRNVVNI GIGGSDLGPA MVCHALDHYA VENVRVHFVS
     NLDPSHLAGT LAQLDPETTL FIVASKTFTT LETLANANSA KAWLLAALRA PEAVARHFVA
     LSTNAQAVEA FGIDPENMFI FWDWVGGRYS LWSAIGLSIA LQIGWGNFQA LLAGAHAMDV
     HFKEAPLEAN MPVILGMLGI WYANFWGTDT YGVFPYDQRL RLLVPFLQQL DMESNGKNVN
     RANKLVNYNT GPIVWGAPGT NGQHAFFELV HQGTRLIPTD FLVAAVNLTP LADQHEWLLA
     NCLAQTEALL KGKSRAVIEA ELIAQGMTRD DARALAPHKV FPGNRPSNTL LYQKLDPHTL
     GMLIALYEHK VFVQGVIWQI NSFDQWGVEL GKQLAPPIRA ALSSVRVIGE HDGSTQGLIA
     DIRRRRGLST