G6PD_DIDVI
ID G6PD_DIDVI Reviewed; 191 AA.
AC P15588;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase;
DE Short=G6PD;
DE EC=1.1.1.49 {ECO:0000250|UniProtKB:P11413};
DE Flags: Fragments;
GN Name=G6PD;
OS Didelphis virginiana (North American opossum) (Didelphis marsupialis
OS virginiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Didelphimorphia; Didelphidae; Didelphis.
OX NCBI_TaxID=9267;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2822568; DOI=10.1016/0888-7543(87)90100-5;
RA Kaslow D.C., Migeon B.R., Persico M.G., Zollo M., Vandeberg J.L.,
RA Samollow P.B.;
RT "Molecular studies of marsupial X chromosomes reveal limited sequence
RT homology of mammalian X-linked genes.";
RL Genomics 1:19-28(1987).
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 -!- SUBUNIT: Homotetramer; dimer of dimers. Interacts with SIRT2; the
CC interaction is enhanced by H(2)O(2) treatment (By similarity).
CC {ECO:0000250|UniProtKB:P11413}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P11413}. Membrane
CC {ECO:0000250|UniProtKB:P11413}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P11413}.
CC -!- PTM: Acetylated by ELP3; acetylation inhibits its homodimerization and
CC enzyme activity. Deacetylated by SIRT2; deacetylation stimulates its
CC enzyme activity (By similarity). {ECO:0000250|UniProtKB:P11413}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; M19637; AAA30971.1; -; Genomic_DNA.
DR EMBL; M19636; AAA30971.1; JOINED; Genomic_DNA.
DR EMBL; M19642; AAA30972.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M19638; AAA30973.1; -; Genomic_DNA.
DR EMBL; M19639; AAA30974.1; -; Genomic_DNA.
DR EMBL; M19641; AAA30975.1; -; Genomic_DNA.
DR EMBL; M19640; AAA30975.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; P15588; -.
DR UniPathway; UPA00115; UER00408.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; 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 InterPro; IPR001282; G6P_DH.
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; 4.
DR Pfam; PF02781; G6PD_C; 1.
DR Pfam; PF00479; G6PD_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW Acetylation; Carbohydrate metabolism; Cytoplasm; Glucose metabolism;
KW Membrane; NADP; Oxidoreductase; Phosphoprotein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT CHAIN 2..191
FT /note="Glucose-6-phosphate 1-dehydrogenase"
FT /id="PRO_0000068082"
FT ACT_SITE 106
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 38..45
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10005"
FT BINDING 163
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT MOD_RES 10
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT MOD_RES 173
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT MOD_RES 179
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT NON_CONS 52..53
FT /evidence="ECO:0000305"
FT NON_CONS 100..101
FT /evidence="ECO:0000305"
FT NON_CONS 131..132
FT /evidence="ECO:0000305"
SQ SEQUENCE 191 AA; 21941 MW; E838F22AA83F4AFD CRC64;
MAEQVALSRT QVCGILREEL YQGDAFHQSD THIFIIMGAS GDLAKKKIYP TIEPASFQRL
NTHMNSLHHG AQANRLFYLA LPPIVYEAVT KNIKETCMSQ DVMQNHLLQM LCLVAMEKPA
STNSDDVRDE KDELQEAWRI FTPLLHHIER EKTQPIPYVY GSRGPPEADE LMKRVGFQYE
GTYKWVNPHK L
