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Database: UniProt
Entry: I3EJY4_NEMP3
LinkDB: I3EJY4_NEMP3
Original site: I3EJY4_NEMP3 
ID   I3EJY4_NEMP3            Unreviewed;       586 AA.
AC   I3EJY4;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000256|ARBA:ARBA00020444};
DE            EC=1.1.1.49 {ECO:0000256|ARBA:ARBA00013019};
DE   Flags: Fragment;
GN   ORFNames=NEQG_00301 {ECO:0000313|EMBL:EIJ89531.1};
OS   Nematocida parisii (strain ERTm3) (Nematode killer fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nematocida.
OX   NCBI_TaxID=935791 {ECO:0000313|EMBL:EIJ89531.1, ECO:0000313|Proteomes:UP000002872};
RN   [1] {ECO:0000313|EMBL:EIJ89531.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ERTm3 {ECO:0000313|EMBL:EIJ89531.1};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cuomo C., Troemel E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.,
RA   Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Nematocida parisii strain ERTm3.";
RL   Submitted (JAN-2011) 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. The main function of this enzyme is
CC       to provide reducing power (NADPH) and pentose phosphates for fatty acid
CC       and nucleic acid synthesis. {ECO:0000256|ARBA:ARBA00025382}.
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   -!- 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}.
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DR   EMBL; GL870876; EIJ89531.1; -; Genomic_DNA.
DR   AlphaFoldDB; I3EJY4; -.
DR   STRING; 935791.I3EJY4; -.
DR   EnsemblFungi; EIJ89531; EIJ89531; NEQG_00301.
DR   VEuPathDB; MicrosporidiaDB:NEQG_00301; -.
DR   HOGENOM; CLU_032837_0_0_1; -.
DR   InParanoid; I3EJY4; -.
DR   OMA; NTSGACR; -.
DR   UniPathway; UPA00115; UER00408.
DR   Proteomes; UP000002872; 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; 2.
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   PANTHER; PTHR23429:SF0; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE; 1.
DR   PANTHER; PTHR23429; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE G6PD; 1.
DR   Pfam; PF02781; G6PD_C; 2.
DR   Pfam; PF00479; G6PD_N; 1.
DR   PRINTS; PR00079; G6PDHDRGNASE.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022526};
KW   Glucose metabolism {ECO:0000256|ARBA:ARBA00022526};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002872}.
FT   DOMAIN          105..243
FT                   /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00479"
FT   DOMAIN          255..434
FT                   /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02781"
FT   DOMAIN          498..578
FT                   /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02781"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EIJ89531.1"
SQ   SEQUENCE   586 AA;  66855 MW;  987902881FA664A4 CRC64;
     MIIIAGCTGD LSKKKLFPAI NKLFRRELYN CTNTNYTNKE LDLTDATLSS STSAHNLSKY
     SPITHANPKD SKCNKNYLEA TESKILYKKI LQGDLLINNN IKIPRIIGYA RSILNSTQFI
     QRIDPNISYL KETISNIEYY SGEYKDMVSN IYGMINEEYN MDSTVSNEPI YFYLAVPPEI
     YPSILKSVKI LKNNGNNGIF KLPILLIEKP IGTSLNSFLQ LKQDILSDLD RSLCVDHYLF
     KNVMVMYKDL YTTSVLQDII VPEHISEVKA YFNEVIGVSG RESYYNTSGA CRDVLQNHLL
     LIISTVLAGT NSRLSILQDI TALTEGGTVF GVYKEYYKVI SRSISVCDSV RESYSETSLE
     KISKIKNIPN KEIKNNGNIK NTDVKETFIR TVTKIGGNWN IPLKMTAGKK MPSHFVGVIL
     IMKKSGILKF AKQKTDVKDY ENLKLLEKII KKLENPSKLD QDTQDISLSD DICVETDESV
     NESEESTENF DKTKNTKKTT ISGKIKIKIT PKEEISVELK YKNKLAKKVN IPIPKTEDKI
     DAYEHLFHQL IFKEDYSNFS ALSEIEEQWR IVDPILDSEN IRRVYY
//
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