ID   G6PI_NITOC              Reviewed;         549 AA.
AC   Q3JCN1;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 95.
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=Noc_0903;
OS   Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB
OS   11848 / C-107).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Nitrosococcus.
OX   NCBI_TaxID=323261;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB 11848 / C-107;
RX   PubMed=16957257; DOI=10.1128/aem.00463-06;
RA   Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J.,
RA   Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T.,
RA   Vergez L.M., Ward B.B.;
RT   "Complete genome sequence of the marine, chemolithoautotrophic, ammonia-
RT   oxidizing bacterium Nitrosococcus oceani ATCC 19707.";
RL   Appl. Environ. Microbiol. 72:6299-6315(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; CP000127; ABA57415.1; -; Genomic_DNA.
DR   RefSeq; WP_002810426.1; NC_007484.1.
DR   AlphaFoldDB; Q3JCN1; -.
DR   SMR; Q3JCN1; -.
DR   STRING; 323261.Noc_0903; -.
DR   KEGG; noc:Noc_0903; -.
DR   eggNOG; COG0166; Bacteria.
DR   HOGENOM; CLU_017947_3_1_6; -.
DR   InParanoid; Q3JCN1; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000006838; 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..549
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_0000230921"
FT   ACT_SITE        354
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        385
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        513
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   549 AA;  61868 MW;  AEC8680882E60C14 CRC64;
     MKPYLAQARS WASLLQHYGC IKKQHMRDLF AADPQRFDKF SLIFNGILFD FSKNRITEET
     LKLLLDLARE RELQQGISRM FAGEPINNTE NRPVLHVALR NRANRPIMVK GKDVMPQVNV
     VLERMGKFCD RVHRGQWRGF SGERLTDIVN IGIGGSDLGP AMVTEALQPY AKSGFRVHFV
     SNIDGTQLAE TLKTIRPETA LFVISSKTFT TQETLTNAHS ARNWFLRAAP DDKAIAKHFI
     AVSTNRSEVE KFGIDPCNMF EFWDWVGGRY SLWSAIGLSI ALYLGMENFE QLLEGAHEMD
     KHFQETPLKQ NIPVIAALVG IWNINFLGAQ SHAVLPYDQY LERFPAYLQQ LEMESNGKHV
     TRGGASVNYA TGNVIWGAPG TNGQHAFFQL LHQGTPLITA DFLASAESHN PLGEHHQILL
     SNFFAQTEAL MKGKDEAEVR AELEEANLAK GEVEALIPHK LFDGNRPSNS FLFSKLTPWT
     LGALIAFYEH KVFTQGLIWD INSFDQWGVE LGKQLATTIL PELQGGEEVN SHDSSTNGLI
     NYYKRIRHL
//