ID A0A2U3Y6S8_LEPWE Unreviewed; 483 AA.
AC A0A2U3Y6S8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000256|RuleBase:RU362120};
DE EC=1.1.1.49 {ECO:0000256|RuleBase:RU362120};
GN Name=G6PD {ECO:0000313|RefSeq:XP_006739426.1};
OS Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Leptonychotes.
OX NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006739426.1};
RN [1] {ECO:0000313|RefSeq:XP_006739426.1}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_006739426.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- 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}.
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DR RefSeq; XP_006739426.1; XM_006739363.2.
DR AlphaFoldDB; A0A2U3Y6S8; -.
DR STRING; 9713.A0A2U3Y6S8; -.
DR GeneID; 102750537; -.
DR KEGG; lww:102750537; -.
DR CTD; 2539; -.
DR OrthoDB; 989808at2759; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000245341; Unplaced.
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:UP000245341}.
FT DOMAIN 7..178
FT /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF00479"
FT DOMAIN 180..471
FT /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02781"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10005"
SQ SEQUENCE 483 AA; 55755 MW; A3255FD8C20C809A CRC64;
MSGEQLADGD LAKKKIYPTI WWLFRDGLLP EDTFIVGYAR SRLTVADIRK QSEPFFKATP
EEKPKLEEFF ARNSYVAGQY DDTASYERLN SHMNALHQGP QANRLFYLAL PPTVYEAVTK
NIHETCMSQT GWNRVIVEKP FGRDLQSSDR LSNHISSLFR EDQIYRIDHY LGKEMVQNLM
VLRFANRIFG PIWNRDNIAC IILTFKEPFG TEGRGGYFDE FGIIRDVMQN HLLQMLCLVA
MEKPASTDSD DVRDEKVKVL KCISEVQADN VVLGQYVGNP SGEGESTKGY LDDPTVPRGS
TTATFAAVVL YVENERWDGV PFILRCGKAL NERKAEVRLQ FRDVAGDIFQ QQCKRNELVI
RVQPNEAVYT KMMTKKPGMF FNPEESELDL TYGNRYKNVK LPDAYERLIL DVFCGNQMHF
VRSDELREAW RIFTPLLHKI EREKLQPIPY VYGSRGPAEA DELMKRVGFQ YEGTYKWVNP
HKL
//
