G6PD_CYBJA
ID G6PD_CYBJA Reviewed; 495 AA.
AC P11410;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase;
DE Short=G6PD;
DE EC=1.1.1.49 {ECO:0000250|UniProtKB:P11413};
OS Cyberlindnera jadinii (Torula yeast) (Pichia jadinii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX NCBI_TaxID=4903;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=8444164; DOI=10.1111/j.1432-1033.1993.tb17630.x;
RA Jeffery J., Persson B., Wood I., Bergman T., Jeffery R., Joernvall H.;
RT "Glucose-6-phosphate dehydrogenase. Structure-function relationships and
RT the Pichia jadinii enzyme structure.";
RL Eur. J. Biochem. 212:41-49(1993).
RN [2]
RP PROTEIN SEQUENCE OF 177-187.
RC STRAIN=ATCC 9950 / CBS 5609 / DSM 2361 / NBRC 0998 / NRRL Y-900;
RX PubMed=2499329; DOI=10.1016/s0006-291x(89)80143-3;
RA Jeffery J., Wood I., McLeod A., Jeffery R., Joernvall H.;
RT "Glucose-6-phosphate dehydrogenase. Characterization of a reactive lysine
RT residue in the Pichia jadinii enzyme reveals a limited structural variation
RT in a functionally significant segment.";
RL Biochem. Biophys. Res. Commun. 160:1290-1295(1989).
RN [3]
RP PROTEIN SEQUENCE OF 1-10, AND ACETYLATION AT SER-1.
RX PubMed=8706859; DOI=10.1016/0014-5793(96)00657-6;
RA Bergman T., Gheorghe M.T., Hjelmqvist L., Joernvall H.;
RT "Alcoholytic deblocking of N-terminally acetylated peptides and proteins
RT for sequence analysis.";
RL FEBS Lett. 390:199-202(1996).
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. The main function of this enzyme is
CC to provide reducing power (NADPH) and pentose phosphates for fatty acid
CC and nucleic acid synthesis (By similarity).
CC {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 -!- 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 -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000305}.
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DR PIR; S11078; S11078.
DR PIR; S29381; S29381.
DR AlphaFoldDB; P11410; -.
DR SMR; P11410; -.
DR iPTMnet; P11410; -.
DR PRIDE; P11410; -.
DR UniPathway; UPA00115; UER00408.
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 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 1: Evidence at protein level;
KW Acetylation; Carbohydrate metabolism; Direct protein sequencing;
KW Glucose metabolism; NADP; Oxidoreductase.
FT CHAIN 1..495
FT /note="Glucose-6-phosphate 1-dehydrogenase"
FT /id="PRO_0000068105"
FT ACT_SITE 241
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P11411"
FT BINDING 15..22
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 49
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 149
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 179..183
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 335
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 369
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT MOD_RES 1
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:8706859"
FT VARIANT 107
FT /note="H -> G"
FT VARIANT 138
FT /note="P -> M"
FT VARIANT 416
FT /note="I -> T"
SQ SEQUENCE 495 AA; 57029 MW; B6944216F4B4C8D8 CRC64;
SYDSFGDRVT IIVFGASGDL ARKKTFPALF GLFREKQLPS TVQIIGYARS HLSDKDFKDY
ISSHFKGGDD KTKEDFLNLC SYISDPYDTD EGYKKLEARC QEYESKHNVK VPERLFYLAL
PPSVFHTVCE QVKKNVYPKN EKSRIIIEKP FGRDLETYRE LQKQISPLFT EDEVYRIDHY
LGKEMVKNLL VLRFGNELFS GIWNNKHITS VQISFKEAFG TEGRGGYFDN IGIIRDVMQN
HLLQVLTLLT MERPVSFDPE AVRDEKVKVL KAFDKIDVND VLLGQYGKSE DGTKPGYLDD
STVKPNSKAV TYAAFRVNIH NERWDGVPIV LRAGKALDEG KAEIRIQFKP VAKGMFKEIQ
RNELVIRIQP NEAIYLKINS KIPGISTETS LTDLDLTYST RYSKDFWIPE AYEALIRDCY
LGNHSNFVRD DELEVSWKLF TPLLEAVEKE ENVKLESYPY GSKGPKELRK YLIDHGYVFN
DPGTYQWPLT NTDVK
