ID A0A0B7NTF9_9FUNG Unreviewed; 554 AA.
AC A0A0B7NTF9;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|ARBA:ARBA00011952, ECO:0000256|RuleBase:RU000612};
DE EC=5.3.1.9 {ECO:0000256|ARBA:ARBA00011952, ECO:0000256|RuleBase:RU000612};
GN Name=PARPA_12837.1 scaffold 45468 {ECO:0000313|EMBL:CEP18533.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP18533.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP18533.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP18533.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-2014) 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; LN733835; CEP18533.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7NTF9; -.
DR STRING; 35722.A0A0B7NTF9; -.
DR OrthoDB; 1657888at2759; -.
DR UniPathway; UPA00109; UER00181.
DR Proteomes; UP000054107; 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:UP000054107}.
SQ SEQUENCE 554 AA; 62763 MW; B4CE50298C940CF7 CRC64;
MVLANKLNTW SKLQQHYDAE GKDIVIKEQF DKDPERFAKY HRVFKGVKTN TSILFDFSKN
RVTDDTLQLL LELAKEADVE KMRNKMFKGE HINFTENRAV LHVALRNLSN EPIYDNGKDV
MPEVREVLEH MKEFSESVRS GEWKGYTGER ITDIVNIGIG GSDLGPVMVT EALKPYAHKD
LKPHYVSNID GTHLAEVLKS IKPETTLFII ASKTFTTQET ITNAESAKAW FLATAKETSH
VAKHFVALST NTELVTKFGI DAKNMFKFWD WVGGRYSLWS AIGLSIAITI GYENFEDLLR
GGHEMDQHFL NTPLENNIPV LMALVGVWYN NFFGAQTEAI LPYDQYMHRF PAYFQQGNME
SNGKYVSRSG EEVQAQTGPI IWGEPGTNGQ HAFYQLIHQG TKMIPCDFLA PIETFNPISK
GVHHDILLSN FFAQTEALMV GKNEQQVRAE MGNNVQENIV PHKVFKGNKP TNSFMFQKLT
PATLGSLIAM YEHKIFVQGA IWDINSYDQW GVELGKQLAK AILPELTTSG TVESHDGSTN
GLINYYKKNK KQYN
//
