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
//