ID A0A0V1CYV8_TRIBR Unreviewed; 537 AA.
AC A0A0V1CYV8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000256|ARBA:ARBA00020444, ECO:0000256|RuleBase:RU362120};
DE EC=1.1.1.49 {ECO:0000256|ARBA:ARBA00013019, ECO:0000256|RuleBase:RU362120};
GN Name=gspd-1 {ECO:0000313|EMBL:KRY54350.1};
GN ORFNames=T03_15596 {ECO:0000313|EMBL:KRY54350.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY54350.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY54350.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY54350.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the rate-limiting step of the oxidative pentose-
CC phosphate pathway, which represents a route for the dissimilation of
CC carbohydrates besides glycolysis. {ECO:0000256|RuleBase:RU362120}.
CC -!- FUNCTION: Cytosolic glucose-6-phosphate dehydrogenase that catalyzes
CC the first and rate-limiting step of the oxidative branch within the
CC pentose phosphate pathway/shunt, an alternative route to glycolysis for
CC the dissimilation of carbohydrates and a major source of reducing power
CC and metabolic intermediates for fatty acid and nucleic acid
CC biosynthetic processes. {ECO:0000256|ARBA:ARBA00002914}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-
CC lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:61548; EC=1.1.1.49;
CC Evidence={ECO:0000256|ARBA:ARBA00001220};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15842;
CC Evidence={ECO:0000256|ARBA:ARBA00001220};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 1/3. {ECO:0000256|ARBA:ARBA00004937, ECO:0000256|RuleBase:RU362120}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009975, ECO:0000256|RuleBase:RU362120}.
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:KRY54350.1}.
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DR EMBL; JYDI01000071; KRY54350.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1CYV8; -.
DR STRING; 45882.A0A0V1CYV8; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_00966; G6PD; 1.
DR InterPro; IPR001282; G6P_DH.
DR InterPro; IPR019796; G6P_DH_AS.
DR InterPro; IPR022675; G6P_DH_C.
DR InterPro; IPR022674; G6P_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR00871; zwf; 1.
DR PANTHER; PTHR23429:SF0; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE; 1.
DR PANTHER; PTHR23429; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE G6PD; 1.
DR Pfam; PF02781; G6PD_C; 1.
DR Pfam; PF00479; G6PD_N; 1.
DR PIRSF; PIRSF000110; G6PD; 1.
DR PRINTS; PR00079; G6PDHDRGNASE.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU362120};
KW Glucose metabolism {ECO:0000256|ARBA:ARBA00022526,
KW ECO:0000256|RuleBase:RU362120}; NADP {ECO:0000256|RuleBase:RU362120};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362120};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653}.
FT DOMAIN 38..230
FT /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF00479"
FT DOMAIN 232..523
FT /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02781"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10005"
SQ SEQUENCE 537 AA; 62151 MW; 2E1941A7EDBCE534 CRC64;
MYKRQMSEPF CCQLTPETIR VIKETLPNEE ELIPHVFVIF GASGDLAKRK TYPTLWWLFR
DRLLPPGTYF IGYARTALTV EQLKENFFPF CHVNFLLITT INCMAVQKDE EDLFESFIKR
NSYICGSYDK EDGFIRLKVE IETVGSRLGA CPNRIFYLAL PPSVYCTVTT NIQKICTCKS
ANAWTRVILE KPFGKDTQSS YELAKHLSGL FNEDQLYRID HYLGKEMVQN LMVLRFANRI
FAPSWNREHI SSVTISFKEP IGTYGRGGYF DEYGIVRDVM QNHVLQMLCL VAMEKPISLQ
AEDIRDEKVR VLKCIAPISA DDMVLGQYVG NSESDIEEQR ISYVDDPKVA KDSVTPTYAL
AVCRINNERW DGVPFFLRCG KALNERKAEV RIQYREVPCD IFPAGQVKRN ELVIRVQPNE
AVYAKLITKQ PGMGFDITET ELDLTYHERY KDIHLPDAYE RLLLEVFCGS QINFVRSDEL
EQAWRIFTPC LHDIEKNRRK PVLYKFGSRG PAEADELMRQ NGFLFTGTYK WKPLSSR
//
