G6PD_BOSIN
ID G6PD_BOSIN Reviewed; 515 AA.
AC Q7YS37;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase;
DE Short=G6PD;
DE EC=1.1.1.49 {ECO:0000250|UniProtKB:P11413};
GN Name=G6PD;
OS Bos indicus (Zebu).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9915;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Ravi Kumar G.V.P.P.S., Sharma A., Suryanarayana V.V.S., Ravi Kumar P.;
RT "Molecular characterization of g6pd in cattle.";
RL Submitted (JUN-2003) 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 -!- 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 at Lys-403; acetylation inhibits its
CC homodimerization and enzyme activity. Deacetylated by SIRT2 at Lys-403;
CC deacetylation stimulates its enzyme activity (By similarity).
CC {ECO:0000250|UniProtKB:P11413}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000305}.
CC -!- CAUTION: Pro-263 is present instead of the conserved His which is
CC expected to act as the active site proton acceptor. {ECO:0000305}.
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DR EMBL; AJ566767; CAD97761.1; -; mRNA.
DR AlphaFoldDB; Q7YS37; -.
DR SMR; Q7YS37; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000515132; Genome assembly.
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 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 2: Evidence at transcript level;
KW Acetylation; Carbohydrate metabolism; Cytoplasm; Glucose metabolism;
KW Hydroxylation; Membrane; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT CHAIN 2..515
FT /note="Glucose-6-phosphate 1-dehydrogenase"
FT /id="PRO_0000068080"
FT BINDING 38..45
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 201..205
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 357
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 360
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 366
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 370
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 393
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 395
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 401..403
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 421..423
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 487
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 503
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 509
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 89
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT MOD_RES 171
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT MOD_RES 171
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT MOD_RES 403
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT MOD_RES 432
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT MOD_RES 497
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT MOD_RES 503
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P11413"
SQ SEQUENCE 515 AA; 59584 MW; 2397324759DD9972 CRC64;
MAEQVALSQT QTCGILWEEL CQSYSFHQSD THIFIIMGAS GDLAKRNIYP TIWWLFQDGL
LPKDTFIVGY TDSHFTVANI RKQSEPFFKS TPEEEPKLEE FFAHSSYMAS QYDDVASYEH
LNSGMNALHQ GPQANCLFYL ALLPSGYRTV TKNICDTCTS QTGWNRIIVE KPFGRDLQSS
NQLSNHIASL FHEDQIYRID HYLGKEVVQN LMVLRFVNRI LGPIWNRDNI ACMSFTFKEP
FGTEGRWSYL SESGIIWEVM QNPLLQILCL VAMEKPISTN SDNIRDDKVR VLKCISKVQV
SNVVLSQYME NPTEEGEATR GYPEDPRVPH GSTTDTFAAA VLYVENERWD GVPFILRCGK
ALNERKAEVR LQFRDVAGDI FRQQCKRNEL VIRVQPNEAV YTKMMTKKPG MFFNPEESEL
DLTYGNRYKN VKFPDAYERL ILDVFCGSQM HFVRSDELRE AWRIFTPLLH HIEREKARPI
PYVYGSRGPV EADELMKRVG FQYEGTYKWV NPHKL
