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Database: UniProt
Entry: Q3LFI5_PROFR
LinkDB: Q3LFI5_PROFR
Original site: Q3LFI5_PROFR 
ID   Q3LFI5_PROFR            Unreviewed;       299 AA.
AC   Q3LFI5;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|RuleBase:RU000612};
DE            EC=5.3.1.9 {ECO:0000256|RuleBase:RU000612};
DE   Flags: Fragment;
GN   Name=gpi {ECO:0000313|EMBL:CAD48588.1};
OS   Propionibacterium freudenreichii subsp. shermanii.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Propionibacterium.
OX   NCBI_TaxID=1752 {ECO:0000313|EMBL:CAD48588.1};
RN   [1] {ECO:0000313|EMBL:CAD48588.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CIP 103027 {ECO:0000313|EMBL:CAD48588.1};
RA   Dimova D.;
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAD48588.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CIP 103027 {ECO:0000313|EMBL:CAD48588.1};
RA   Meurice G.;
RT   "Metabolic reconstruction of glycolysis pathway in Propionibacterium
RT   shermanii.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU000612};
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|RuleBase:RU000612}.
CC   -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|ARBA:ARBA00006604,
CC       ECO:0000256|RuleBase:RU000612}.
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DR   EMBL; AJ508909; CAD48588.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3LFI5; -.
DR   UniPathway; UPA00109; UER00181.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05015; SIS_PGI_1; 1.
DR   InterPro; IPR001672; G6P_Isomerase.
DR   InterPro; IPR018189; Phosphoglucose_isomerase_CS.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   InterPro; IPR035476; SIS_PGI_1.
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; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE   3: Inferred from homology;
KW   Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432,
KW   ECO:0000256|RuleBase:RU000612};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU000612};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU000612}.
FT   NON_TER         299
FT                   /evidence="ECO:0000313|EMBL:CAD48588.1"
SQ   SEQUENCE   299 AA;  33026 MW;  4AB5F688B27DF4C6 CRC64;
     MNSPVDPTST PAWAELENLH RSLDVDFRKW FAEEPNRAQQ FTLRAGDLTV DLSRNYLNQQ
     VRDTLVSLAA QVDLAGRRDA MFRGDRINTT EDRSVLHVAL RLPKGAELDV DGVNVVDQVH
     EVLDREISFT EAVRSGERGG VTGKPITTVV NIGIGGSDLG PVMVYEALKP YKHDRIECRF
     ISNIDPADMY EKTHDLDAET TLFIVASKTF TTLETMTNAR MAKNWLINSL QSSGAIDGTA
     DSRARAIKRH FVAVSTNAEK VSEFGIDHAN MFGFWDWVGG RYSVDSAVGL SALIAIGPD
//
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