ID G4TTS3_SERID Unreviewed; 549 AA.
AC G4TTS3;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|ARBA:ARBA00018388, ECO:0000256|RuleBase:RU000612};
DE EC=5.3.1.9 {ECO:0000256|ARBA:ARBA00011952, ECO:0000256|RuleBase:RU000612};
GN ORFNames=PIIN_08676 {ECO:0000313|EMBL:CCA74716.1};
OS Serendipita indica (strain DSM 11827) (Root endophyte fungus)
OS (Piriformospora indica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Sebacinales; Serendipitaceae; Serendipita.
OX NCBI_TaxID=1109443 {ECO:0000313|EMBL:CCA74716.1, ECO:0000313|Proteomes:UP000007148};
RN [1] {ECO:0000313|EMBL:CCA74716.1, ECO:0000313|Proteomes:UP000007148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11827 {ECO:0000313|EMBL:CCA74716.1,
RC ECO:0000313|Proteomes:UP000007148};
RX PubMed=22022265; DOI=10.1371/journal.ppat.1002290;
RA Zuccaro A., Lahrmann U., Guldener U., Langen G., Pfiffi S., Biedenkopf D.,
RA Wong P., Samans B., Grimm C., Basiewicz M., Murat C., Martin F.,
RA Kogel K.H.;
RT "Endophytic Life Strategies Decoded by Genome and Transcriptome Analyses of
RT the Mutualistic Root Symbiont Piriformospora indica.";
RL PLoS Pathog. 7:e1002290-e1002290(2011).
CC -!- FUNCTION: In the cytoplasm, catalyzes the conversion of glucose-6-
CC phosphate to fructose-6-phosphate, the second step in glycolysis, and
CC the reverse reaction during gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00024178}.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCA74716.1}.
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DR EMBL; CAFZ01000346; CCA74716.1; -; Genomic_DNA.
DR AlphaFoldDB; G4TTS3; -.
DR STRING; 1109443.G4TTS3; -.
DR eggNOG; KOG2446; Eukaryota.
DR HOGENOM; CLU_017947_3_1_1; -.
DR InParanoid; G4TTS3; -.
DR OMA; DWYRQLW; -.
DR OrthoDB; 1657888at2759; -.
DR UniPathway; UPA00109; UER00181.
DR Proteomes; UP000007148; Unassembled WGS sequence.
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 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007148}.
SQ SEQUENCE 549 AA; 60900 MW; B2E1BB88D3AB4F56 CRC64;
MPGTLASDYA AWSKLQQLYD SKKQSLVLKD LFAADPDRFK KFSREYSAPN ASFLLDFSKN
LIDEEVFAAL IQLVKEADVE GARDAMFRGE HINTSEDRAV LHIALRNVGN TFTISEPGVD
EVQGVLEHMR VFSDSIRSGE WKGYTGKSIN TIVNIGIGGS DLGPVMVTEA LKYYSKRDLR
AFFVSNIDGT HIAETLKECD PETTLFIIAS KTFTTQETIT NAETAKEWFL KKAGDKAHVA
KHFVALSTNT KAVTAFGIAE ENMFQFWDWV GGRYSLWSAI GLSIALVIGF DNFKALLEGA
HEMDKHFTST PLENNLPVIM AALGIWYGDF YGSQTHVLLP YDQYLHKFAD YFQQGDMESN
GKFVTKAGQR VNYQTGPIIW GAAGTNGQHS FYQLLHQGTK LIPADFLAPA NSLNDVGGDK
HHRILLSNFF AQPEALAFGK NEETVKKELG PNASEALIKS KVFEGNRPSN SIMFPKMTPS
TLGALIALYE HKIFVQGMVW GINSFDQMGV ELGKILAKNI LAQLNSPEDV VGHDSSTTGL
IHYYQKNRA
//
