ID W9QW92_9ROSA Unreviewed; 598 AA.
AC W9QW92;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000256|RuleBase:RU362120};
DE EC=1.1.1.49 {ECO:0000256|RuleBase:RU362120};
GN ORFNames=L484_017470 {ECO:0000313|EMBL:EXB40328.1};
OS Morus notabilis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX NCBI_TaxID=981085 {ECO:0000313|EMBL:EXB40328.1, ECO:0000313|Proteomes:UP000030645};
RN [1] {ECO:0000313|Proteomes:UP000030645}
RP NUCLEOTIDE SEQUENCE.
RA He N., Zhao S.;
RT "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KE343766; EXB40328.1; -; Genomic_DNA.
DR RefSeq; XP_010090664.1; XM_010092362.1.
DR AlphaFoldDB; W9QW92; -.
DR STRING; 981085.W9QW92; -.
DR GeneID; 21400465; -.
DR KEGG; mnt:21400465; -.
DR eggNOG; KOG0563; Eukaryota.
DR OrthoDB; 312822at2759; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000030645; Unassembled WGS sequence.
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:SF11; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE 2, 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 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:UP000030645}.
FT DOMAIN 116..294
FT /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF00479"
FT DOMAIN 297..591
FT /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02781"
FT BINDING 289
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10005"
SQ SEQUENCE 598 AA; 67608 MW; D16BAD11BF813A47 CRC64;
MAALSSAQSC RIYSSLPSSS SSSSSSLTSL QRIAVSSPAT KRFLPAKVSL QSQPVSHRNV
VRMQQDVATT VTVVGNDTPF NKLKEGILSV TSSEESKEAA GIDDDNGNES TVSITVVGAS
GDLAKKKIFP ALFALYYEDW LPKHFTVYGY ARSKMTDAEL RNMVSKTLTC RIDKRENCGE
KMDQFLKRCF YHSGQYDSQQ NFEDLDKKLK EHEAGRVSNR LFYLSIPPNI FIDAVRCASM
SASSGNGWTR VIVEKPFGRD SESSAALTKA LKQYLEEEQI FRIDHYLGKE LVENLSVLRF
SNLIFEPLWS RQYIRNVQLI FSEDFGTEGR GGYFNNYGII RDIMQNHLLQ ILALFAMETP
VSLDAEDIRN EKVKVLRSMR PLQLENVVVG QYKSHTKGGV TYPAYTDDKT VPKDSLTPTF
AAAALFIDNA RWDGVPFLMK AGKALHNKWA EIRVQFRRVP GNLYNRNFGT DFDRATNELV
IRVQPDEAIY LKINNKVPGL GMRLDRSNLN LLYAARYSKE IPDAYERLLL DAIEGERRLF
IRSDELDAAW ALFTPLLKEL EEKKIIPEYY PYGSRGPVGA HYLAARYNVR WGDVGVEQ
//
