ID A0A2I4DP46_JUGRE Unreviewed; 509 AA.
AC A0A2I4DP46;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000256|RuleBase:RU362120};
DE EC=1.1.1.49 {ECO:0000256|RuleBase:RU362120};
GN Name=LOC108982085 {ECO:0000313|RefSeq:XP_018808910.2,
GN ECO:0000313|RefSeq:XP_035548817.1};
OS Juglans regia (English walnut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Juglandaceae; Juglans.
OX NCBI_TaxID=51240 {ECO:0000313|Proteomes:UP000235220, ECO:0000313|RefSeq:XP_018808910.2};
RN [1] {ECO:0000313|RefSeq:XP_018808910.2, ECO:0000313|RefSeq:XP_035548817.1}
RP IDENTIFICATION.
RC TISSUE=Leaves {ECO:0000313|RefSeq:XP_018808910.2,
RC ECO:0000313|RefSeq:XP_035548817.1};
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:ARBA00000740,
CC ECO:0000256|RuleBase:RU362120};
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_018808910.2; XM_018953365.2.
DR RefSeq; XP_035548817.1; XM_035692924.1.
DR OrthoDB; 312822at2759; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000235220; Chromosome 1.
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:0009051; P:pentose-phosphate shunt, oxidative branch; IEA:UniProt.
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:SF13; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE 1, CHLOROPLASTIC; 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:UP000235220}.
FT DOMAIN 26..204
FT /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF00479"
FT DOMAIN 207..501
FT /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02781"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10005"
SQ SEQUENCE 509 AA; 58307 MW; B22290210768ADA9 CRC64;
MEPQGKEESL PFSQSENLGP QLSITVVGAS GDLAKKKIFP ALFALYYEDW LPENFIVFGY
ARTKMTDEEL RNMISRTLTC RIDQRENCEE KMDRFLKRCF YHSGQYNSEE HFAELNRKLQ
EKEAGKLSNR LFYLSIPPNI FVDVVKCASL RASSTSGWTR VIVEKPFGRD SESSGELTRC
LKLYLTEDQI FRIDHYLGKE LVENLSVLRF SNLVFEPLWS RNFIRSVQLI FSEDFGTEGR
GGYFDNYGII RDIMQNHLLQ ILALFAMETP VSLDAEDIRN EKVKVLRSMR PLQLDDVAVG
QYKGHSKGGK SYPAYIDDPT VPNNSLTPTF AAAALFINNA RWDGVPFLMK AGKALHTKRA
EIRVQFRHVP GNLYKRNFGT DLDKATNELV LRVQPDEAIY LKINNKVPGL GMRLDRSDLN
LLYRARYSRE IPDAYERLLL DAVEGERRLF IRSDELDAAW ALFTPLLKEL EQKKIVPELY
PYGSRGPVGA HYLAAKHNVR WGDLSGEAS
//
