ID   G6PE_RABIT              Reviewed;         763 AA.
AC   P56201;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   16-JUN-2009, entry version 67.
DE   RecName: Full=GDH/6PGL endoplasmic bifunctional protein;
DE   Includes:
DE     RecName: Full=Glucose 1-dehydrogenase;
DE              EC=1.1.1.47;
DE     AltName: Full=Hexose-6-phosphate dehydrogenase;
DE   Includes:
DE     RecName: Full=6-phosphogluconolactonase;
DE              Short=6PGL;
DE              EC=3.1.1.31;
GN   Name=H6PD; Synonyms=GDH;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=New Zealand white; TISSUE=Liver;
RX   MEDLINE=93281746; PubMed=8506377; DOI=10.1073/pnas.90.11.5302;
RA   Ozols J.;
RT   "Isolation and the complete amino acid sequence of lumenal endoplasmic
RT   reticulum glucose-6-phosphate dehydrogenase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:5302-5306(1993).
CC   -!- FUNCTION: Oxidizes glucose-6-phosphate and glucose, as well as
CC       other hexose-6-phosphates (By similarity).
CC   -!- CATALYTIC ACTIVITY: Beta-D-glucose + NAD(P)(+) = D-glucono-1,5-
CC       lactone + NAD(P)H.
CC   -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate + NAD(P)(+) = D-glucono-
CC       1,5-lactone 6-phosphate + NAD(P)H.
CC   -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6-
CC       phospho-D-gluconate.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CC       Note=Microsomes, endoplasmic reticulum lumen.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the glucose-6-
CC       phosphate dehydrogenase family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       glucosamine/galactosamine-6-phosphate isomerase family. 6-
CC       phosphogluconolactonase subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=Ref.1; Type=Miscellaneous discrepancy; Note=The sequence was incorrect due to the transposition of a section that was put in position 330 to 436 and which is now transposed to position 593 to 700;
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DR   HSSP; P11413; 1QKI.
DR   Ensembl; ENSOCUG00000000798; Oryctolagus cuniculus.
DR   HOVERGEN; P56201; -.
DR   BRENDA; 1.1.1.47; 255.
DR   BRENDA; 3.1.1.31; 255.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:EC.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0047936; F:glucose 1-dehydrogenase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR005900; 6-phosphogluconolactonase.
DR   InterPro; IPR001282; Glc-6-P_DH.
DR   InterPro; IPR019796; Glc-6-P_DH_AS.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR23429; G6PDH; 1.
DR   Pfam; PF02781; G6PD_C; 1.
DR   Pfam; PF00479; G6PD_N; 1.
DR   PRINTS; PR00079; G6PDHDRGNASE.
DR   ProDom; PD001129; G6PD; 1.
DR   TIGRFAMs; TIGR01198; pgl; 1.
DR   PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing;
KW   Endoplasmic reticulum; Glucose metabolism; Glycoprotein; Hydrolase;
KW   Multifunctional enzyme; NAD; NADP; Oxidoreductase; Phosphoprotein;
KW   Pyrrolidone carboxylic acid.
FT   CHAIN         1    763       GDH/6PGL endoplasmic bifunctional
FT                                protein.
FT                                /FTId=PRO_0000068139.
FT   REGION        1    507       Glucose 1-dehydrogenase.
FT   REGION      508    521       Linker.
FT   REGION      522    763       6-phosphogluconolactonase.
FT   ACT_SITE    248    248       Proton acceptor (By similarity).
FT   BINDING      15     15       NADP (By similarity).
FT   BINDING      47     47       NADP (By similarity).
FT   BINDING     185    185       Substrate (By similarity).
FT   BINDING     189    189       Substrate (By similarity).
FT   MOD_RES       1      1       Pyrrolidone carboxylic acid.
FT   MOD_RES     297    297       Phosphotyrosine (By similarity).
FT   CARBOHYD    138    138       N-linked (GlcNAc...).
FT   CARBOHYD    263    263       N-linked (GlcNAc...).
FT   VARIANT      69     69       R -> K.
FT   VARIANT      75     75       L -> R.
SQ   SEQUENCE   763 AA;  85285 MW;  2A4E1039062E8672 CRC64;
     QELQGHVSVI LLGATGDLAK KYLWQGLFQL FLDEAGKGHS FSFHGAALTA PKQGQELMAK
     ALESLSCPRD MAPSLCAELQ AQFLRLSRYR QLKTAEDYQA LGRDIEAQVQ QEGLREAGRM
     FYFSVPPFAY ADIARNINSS CRPGPGAWLR VVLEKPFGHD HLSAQQLATE LGSFFQEEEM
     YRVDHYLGKQ AVAQILPFRD QNRRALDSLW NRHHVERVEI IMKETVDAEG RTSFYEEYGV
     IRDTLQNHLT EILTLVAMEL PANVSCSEAV LRHKLQAFRA LRRLQRGSAV VGQYQTYSEQ
     VRGELRKPAG SPSLTPTFAG VLVHVDNLRM EGVPFILMSG KALDERVGYV RVLFKNQAFC
     AQSEKHWAPA QSRCLPRCII FYIGHGELGH PAVVVSRNLF RPFLPAQSWR EVEDRPGLQL
     FGRPLSDFYA FSPVKERDAY SILLSHIFHA RKESFVPTEH LLASWVFWTP LLESLAREVP
     RLYPGGADSG RLLDFEFSGS HLSFSLGQPE QLVPGPGSTP RPSDFQVLGA KYRESPLISA
     WPDELISKLA SDIEAAAVQA VRRVGTFHLA LSGGSSPIAL FQQLASGHYG FPVPLSDPES
     NFQGLQAHLL QHVRVPYYNI HPMPVNLHQR LCAEEDRGAQ AAYASEISAL VTWCSFDEVL
     QGMGTDGHTA SLFPQSPTGL DGEQLVVLTE SPSRPHQQRR MSLSLPLINR AKKVAVLVMG
     RTKRDITLLV SRVGREPKNW PISGVLPTSG QLVWYMDYEA FLG
//