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Database: UniProt
Entry: F8KQB7_HELBC
LinkDB: F8KQB7_HELBC
Original site: F8KQB7_HELBC 
ID   F8KQB7_HELBC            Unreviewed;       551 AA.
AC   F8KQB7;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 61.
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   OrderedLocusNames=HBZC1_13400 {ECO:0000313|EMBL:CCB80326.1};
OS   Helicobacter bizzozeronii (strain CIII-1).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1002804 {ECO:0000313|EMBL:CCB80326.1, ECO:0000313|Proteomes:UP000008387};
RN   [1] {ECO:0000313|EMBL:CCB80326.1, ECO:0000313|Proteomes:UP000008387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIII-1 {ECO:0000313|EMBL:CCB80326.1,
RC   ECO:0000313|Proteomes:UP000008387};
RX   PubMed=21705603; DOI=10.1128/JB.05439-11;
RA   Schott T., Rossi M., Hanninen M.L.;
RT   "Genome sequence of Helicobacter bizzozeronii strain CIII-1, an isolate
RT   from human gastric mucosa.";
RL   J. Bacteriol. 193:4565-4566(2011).
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}.
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DR   EMBL; FR871757; CCB80326.1; -; Genomic_DNA.
DR   RefSeq; WP_013890737.1; NC_015674.1.
DR   AlphaFoldDB; F8KQB7; -.
DR   STRING; 1002804.HBZC1_13400; -.
DR   GeneID; 64362430; -.
DR   KEGG; hbi:HBZC1_13400; -.
DR   eggNOG; COG0166; Bacteria.
DR   HOGENOM; CLU_017947_3_1_7; -.
DR   OMA; IGVWYIN; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000008387; 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:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
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 {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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008387}.
FT   ACT_SITE        354
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT   ACT_SITE        385
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT   ACT_SITE        513
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   551 AA;  62495 MW;  46122DB61EF06C37 CRC64;
     MREHLTKLNA FKRLQEHFKA IQNTHMRDMF KEDPERAMRY FLQAGPISLD YSKNRINDET
     LQLLQDLAKE CQLSAKINAM FGGEKINTTE ERAVLHTALR YQGEESIMVE GQDVMPAVRE
     VLARMESFSD ALRCGEWLGY TNQVITDVVN IGIGGSDLGA LMVCKALKRY ASPRLNMYFV
     SNVDGTQIQG VLDKVHPETT LFIVASKTFS TQETLTNALS ARQWFLAHAL DEAHIAKHFV
     AVSTNKQAVK DFGIDTHNMF SFWNWVGGRY SLWSAIGLSI MIYLGKQNFR SLLQGAFEMD
     QHFKEAPFTH NMPVILALLG VWYVNFFDAG SHLIAPYDQY LRYFPRFIQQ LDMESNGKRT
     TLEGEVVDYD TGPIIWGDLG INSQHAFFQL LHQGTHLTPI DFIASLSKEG HLSGHHEILL
     SNLFAQAQAF MKGRDYNQAY EQLLQMGIEE QKARKLASHR VFSGNRPSNV ILLDAITPKS
     IGALIALYEH KIFVQGVIWD INSFDQWGVE LGKELAKDIL AQLHGKQAPN THEDSSTQHL
     ITLYKTFNQG V
//
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