G6PD_DROYA
ID G6PD_DROYA Reviewed; 518 AA.
AC Q27638;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase;
DE Short=G6PD;
DE EC=1.1.1.49 {ECO:0000250|UniProtKB:P11413};
DE Flags: Fragment;
GN Name=Zw; Synonyms=G6pd;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BG1016;
RA Eanes W.F., Kirchner M., Yoon J., Biermann C., Wang I., McCartney M.,
RA Verrelli B.C.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:P11413}.
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:0000250|UniProtKB:P11413};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15842;
CC Evidence={ECO:0000250|UniProtKB:P11413};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 1/3. {ECO:0000250|UniProtKB:P11413}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P11413}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; U42750; AAB02813.1; -; Genomic_DNA.
DR AlphaFoldDB; Q27638; -.
DR SMR; Q27638; -.
DR STRING; 7245.FBpp0260874; -.
DR eggNOG; KOG0563; Eukaryota.
DR UniPathway; UPA00115; UER00408.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; ISS:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006739; P:NADP metabolic process; ISS:UniProtKB.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
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 PANTHER; PTHR23429; PTHR23429; 1.
DR Pfam; PF02781; G6PD_C; 1.
DR Pfam; PF00479; G6PD_N; 1.
DR PIRSF; PIRSF000110; G6PD; 1.
DR PRINTS; PR00079; G6PDHDRGNASE.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00871; zwf; 1.
DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cytoplasm; Glucose metabolism; NADP;
KW Oxidoreductase.
FT CHAIN <1..518
FT /note="Glucose-6-phosphate 1-dehydrogenase"
FT /id="PRO_0000068094"
FT ACT_SITE 261
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 36..43
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 199..203
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 356
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 359
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 365
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 369
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 400..402
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 420..422
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 486
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 502
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 508
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 518 AA; 59938 MW; 6AFA194E1D3A3E8B CRC64;
DHTALDLIIK SLKSPTMVCE GTHFDGKIPH TFVIFGASGD LAKKKIYPKL WWFYRDDLLP
KLTKFCGYAR SMLTVDSIKE QCLPYMKVQS HEQKKYEEFW ALNEYVSGRY DGRTGFELLN
QQLELMENKN KANRIFYLAL PPSVFEEVTV NIKQICMSVC GWNRVIIEKP FGRDDASSQA
LSDHLAALFH EDQLYRIDHY LGKEMVQNLM TIRFGNKILS STWNRENIAS VLITFKEPFG
TQGRGGYFDE FGIIRDVMQN HLLQILSLVA MEKPVSCHPD DIRDEKVKVL KSIETLTLKD
MVLGQYLGNP QGTTDDARTG YVEDPTVSDD SNTPTYALGV LKINNERWQG VPFILRCGKR
LNERKAEVRI QYQDVPGDIF EGNTKRNELV IRVQPGEALY FKMMTKSPGI TFDIEETELD
LTYEHRYKDS YLPDAYERLI LDVFCGSQMH FVRSDQLREA WRIFTPILHQ IEREHIRPIT
YQYGSRGPKE ADRMCEENNF KYSGSYKWHG GKAATSNL
