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Database: UniProt
Entry: D8LVZ7_BLAHO
LinkDB: D8LVZ7_BLAHO
Original site: D8LVZ7_BLAHO 
ID   D8LVZ7_BLAHO            Unreviewed;       480 AA.
AC   D8LVZ7;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=phosphogluconate dehydrogenase (NADP(+)-dependent, decarboxylating) {ECO:0000256|ARBA:ARBA00013011};
DE            EC=1.1.1.44 {ECO:0000256|ARBA:ARBA00013011};
GN   ORFNames=GSBLH_T00000382001 {ECO:0000313|EMBL:CBK19986.2},
GN   GSBLH_T00003921001 {ECO:0000313|EMBL:CBK24154.2};
OS   Blastocystis hominis.
OC   Eukaryota; Sar; Stramenopiles; Bigyra; Opalozoa; Opalinata; Blastocystidae;
OC   Blastocystis.
OX   NCBI_TaxID=12968 {ECO:0000313|EMBL:CBK19986.2};
RN   [1] {ECO:0000313|EMBL:CBK19986.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Singapore isolate B {ECO:0000313|EMBL:CBK19986.2};
RA   Wincker P.;
RT   "Sequencing and annotation of the Blastocystis hominis genome.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the oxidative decarboxylation of 6-phosphogluconate
CC       to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP
CC       to NADPH. {ECO:0000256|ARBA:ARBA00002526}.
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC       3/3. {ECO:0000256|ARBA:ARBA00004874}.
CC   -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00008419}.
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DR   EMBL; FN668638; CBK19986.2; -; Genomic_DNA.
DR   EMBL; FN668683; CBK24154.2; -; Genomic_DNA.
DR   RefSeq; XP_012894034.1; XM_013038580.1.
DR   RefSeq; XP_012898202.1; XM_013042748.1.
DR   AlphaFoldDB; D8LVZ7; -.
DR   EnsemblProtists; CBK19986; CBK19986; GSBLH_T00000382001.
DR   EnsemblProtists; CBK24154; CBK24154; GSBLH_T00003921001.
DR   GeneID; 24917694; -.
DR   GeneID; 24920974; -.
DR   InParanoid; D8LVZ7; -.
DR   UniPathway; UPA00115; UER00410.
DR   Proteomes; UP000008312; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006114; 6PGDH_C.
DR   InterPro; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR006183; Pgluconate_DH.
DR   PANTHER; PTHR11811; 6-PHOSPHOGLUCONATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11811:SF25; 6-PHOSPHOGLUCONATE DEHYDROGENASE, DECARBOXYLATING; 1.
DR   Pfam; PF00393; 6PGD; 1.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   PRINTS; PR00076; 6PGDHDRGNASE.
DR   SMART; SM01350; 6PGD; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Gluconate utilization {ECO:0000256|ARBA:ARBA00023064};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Pentose shunt {ECO:0000256|ARBA:ARBA00023126};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008312};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        414..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          194..476
FT                   /note="6-phosphogluconate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01350"
SQ   SEQUENCE   480 AA;  52559 MW;  C9D79670630778F4 CRC64;
     MSSDIGIYGL STRAINLALN FAAKGLSVSI GHRSSDLIKE CTHQAEKKDL DEKITGKKDV
     NGFCDSLSSP KKVILMSKPG TSAEKNYSKI LAALEEGDLL IDATSEGYEI NLRREKEAAE
     KGVRFLTMEI LGTTKELQKG CGFLLSGERE AYDLVEGPLK KAATEVEYEP CVAYIGNSVS
     AGYAGMALSS LGLGMEQLVA EAYHMLHEAG FTNEEVSKSI NGWNKDSLAS PFLENLLHIL
     KKKDQDVEGC EKGEGSLLDK VLDCPLPRPD HSTLLREGFE HHAAIGALTA AVQEIAVSAK
     REERSKAATL WNGPEFDWQK LDHVQLIEDL RNTFVCGQLV LATQTFALLR RASEDFSWAM
     KLEEVGRVVA GAASFRSGLL VVLKESVENG DLSLLQNEAV SEILQKKQAS WRRVAALAVI
     GGVSAPVATA SLAYYDTMRR DKLPQNVVVA MRDFLEASSF ERTDCARGMT YHCEWTKETN
//
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