ID M2X737_GALSU Unreviewed; 532 AA.
AC M2X737;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000256|RuleBase:RU362120};
DE EC=1.1.1.49 {ECO:0000256|RuleBase:RU362120};
GN ORFNames=Gasu_04100 {ECO:0000313|EMBL:EME32315.1};
OS Galdieria sulphuraria (Red alga).
OC Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC Galdieria.
OX NCBI_TaxID=130081 {ECO:0000313|EMBL:EME32315.1, ECO:0000313|Proteomes:UP000030680};
RN [1] {ECO:0000313|Proteomes:UP000030680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX PubMed=23471408; DOI=10.1126/science.1231707;
RA Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA Lercher M.J., Weber A.P.;
RT "Gene transfer from bacteria and archaea facilitated evolution of an
RT extremophilic eukaryote.";
RL Science 339:1207-1210(2013).
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|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|RuleBase:RU362120}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000256|RuleBase:RU362120}.
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DR EMBL; KB454486; EME32315.1; -; Genomic_DNA.
DR RefSeq; XP_005708835.1; XM_005708778.1.
DR AlphaFoldDB; M2X737; -.
DR STRING; 130081.M2X737; -.
DR EnsemblPlants; EME32315; EME32315; Gasu_04100.
DR GeneID; 17090906; -.
DR Gramene; EME32315; EME32315; Gasu_04100.
DR KEGG; gsl:Gasu_04100; -.
DR eggNOG; KOG0563; Eukaryota.
DR OMA; PDEGIQM; -.
DR OrthoDB; 989808at2759; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000030680; 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: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; 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 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.
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|RuleBase:RU362120,
KW ECO:0000313|EMBL:EME32315.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030680}.
FT DOMAIN 43..223
FT /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF00479"
FT DOMAIN 226..507
FT /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02781"
SQ SEQUENCE 532 AA; 61368 MW; A773543D89112247 CRC64;
MENTSKLLKK SINRLGSNPN LTIMDNDYLA NQTELEQEVT FCVIGASGDL SRKKTMPALF
SLYYHNVLPF KFHIVGFGRK NLSDQSFREA AMENLSCRTG VVDKDECDRK MQQFLQHVHY
VCGQYNSEED FRNLHKFCCR LEQDDDAARL FYLAVPPSVF AFALKNIKLC ATAENGWTRV
IIEKPFGRDS ESYEELRETI SKYFEEDQVY RIDHYVGKEV VQNITTLRFG NYVFESLWNR
KHVRRIDILF KENFGTEGRA GYFDSFGIIR DIMQNHLLQV LAYLTMERPK SFKADDISTE
KTKLIGSIRQ LKAEDFVTGQ YDGYKAEEGV PEDSTTPTFA ACVLHIDNDR WKNVPVLMIA
GKGLDERLAE IRILFRKGLT ESFLHKGDSI GNQIVIRIQP DESISLHILS KVPGLSTELR
ETCLDLTYRD KFEHESKDIA DAYERLILDA IHGEKSLFIY DEQLEASWKL FTPALNELES
EKSRPPLIYK FGDGIPSEVE NLLWKHEAEC GNCIEAEPAL KDFHSNEFRN NL
//
