ID A0A1W5DCD7_9LECA Unreviewed; 552 AA.
AC A0A1W5DCD7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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};
OS Lasallia pustulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC OSLEUM clade; Umbilicariomycetidae; Umbilicariales; Umbilicariaceae;
OC Lasallia.
OX NCBI_TaxID=136370 {ECO:0000313|EMBL:SLM40843.1, ECO:0000313|Proteomes:UP000192927};
RN [1] {ECO:0000313|Proteomes:UP000192927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sharma R., Thines M.;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FWEW01003741; SLM40843.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W5DCD7; -.
DR OrthoDB; 1657888at2759; -.
DR UniPathway; UPA00109; UER00181.
DR Proteomes; UP000192927; 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}.
SQ SEQUENCE 552 AA; 61403 MW; A91A6DBA8A161336 CRC64;
MPGFAQASDL KAWQQLQEHH TNLGRNIVLK EFFAEDPQRF QKFSRTFNNT ADKSEILFDF
SKNFITEETL SLLVQLAKEA DLEKLRDDMF AGKHINFTED RAVYHVALRN VTNDPMEVDG
KSVVEEVNSV LEHMKEFSEQ IRSGEWKGYT GKKIKTIINI GIGGSDLGPV MVSEALKPYG
DRSLTLHFVS NIDGTHIAEA LRASDPETTM FLVASKTFTT AETTTNANTA KSWFLKTAKG
ESHIAKHFVA LSTNEEEVTK FGIDKKNMFG FASWVGGRYS VWSAIGLSVC IYIGFENWKE
FLAGGHAMDM HFKNTPLEEN IPVLGGLLSV WYSDFFGAQT HLVSPFDQYL HRFPAYLQQL
SMESNGKAIT RSGDYVKYTT GAILFGEPAT NAQHSFYQLL HQGTKLIPTD FILAAESHNP
VENNKHQKML ASNFFAQAEA LMVGKTPDEV KAEGAPTELV PHKTFLGNRP TTSILAQKIT
PGTLGALIAY YEHLTFTEGA VWNINSFDQW GVELGKSLAK KILAELEESG ESTKHDASTS
GLINAFKKKA GI
//
