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Database: UniProt
Entry: R9P7L4_PSEHS
LinkDB: R9P7L4_PSEHS
Original site: R9P7L4_PSEHS 
ID   R9P7L4_PSEHS            Unreviewed;       546 AA.
AC   R9P7L4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|RuleBase:RU000485};
DE            EC=1.1.1.44 {ECO:0000256|RuleBase:RU000485};
GN   ORFNames=PHSY_001679 {ECO:0000313|EMBL:GAC94110.1};
OS   Pseudozyma hubeiensis (strain SY62) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX   NCBI_TaxID=1305764 {ECO:0000313|EMBL:GAC94110.1, ECO:0000313|Proteomes:UP000014071};
RN   [1] {ECO:0000313|Proteomes:UP000014071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SY62 {ECO:0000313|Proteomes:UP000014071};
RX   PubMed=23814110; DOI=10.1128/genomea.00409-13;
RA   Konishi M., Hatada Y., Horiuchi J.;
RT   "Draft genome sequence of the basidiomycetous yeast-like fungus Pseudozyma
RT   hubeiensis SY62, which produces an abundant amount of the biosurfactant
RT   mannosylerythritol lipids.";
RL   Genome Announc. 1:E0040913-E0040913(2013).
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-phospho-D-gluconate + NADP(+) = CO2 + D-ribulose 5-phosphate
CC         + NADPH; Xref=Rhea:RHEA:10116, ChEBI:CHEBI:16526, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58121, ChEBI:CHEBI:58349, ChEBI:CHEBI:58759; EC=1.1.1.44;
CC         Evidence={ECO:0000256|ARBA:ARBA00000530,
CC         ECO:0000256|RuleBase:RU000485};
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, ECO:0000256|RuleBase:RU000485}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00008419, ECO:0000256|RuleBase:RU000485}.
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DR   EMBL; DF238782; GAC94110.1; -; Genomic_DNA.
DR   RefSeq; XP_012187697.1; XM_012332307.1.
DR   AlphaFoldDB; R9P7L4; -.
DR   STRING; 1305764.R9P7L4; -.
DR   GeneID; 24106976; -.
DR   eggNOG; KOG2653; Eukaryota.
DR   HOGENOM; CLU_024540_4_2_1; -.
DR   OrthoDB; 3013545at2759; -.
DR   UniPathway; UPA00115; UER00410.
DR   Proteomes; UP000014071; Unassembled WGS sequence.
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; IPR006113; 6PGDH_Gnd/GntZ.
DR   InterPro; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR006184; 6PGdom_BS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR006183; Pgluconate_DH.
DR   NCBIfam; TIGR00873; gnd; 1.
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.
DR   PROSITE; PS00461; 6PGD; 1.
PE   3: Inferred from homology;
KW   Gluconate utilization {ECO:0000256|ARBA:ARBA00023064,
KW   ECO:0000256|RuleBase:RU000485}; NADP {ECO:0000256|RuleBase:RU000485};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000485};
KW   Pentose shunt {ECO:0000256|ARBA:ARBA00023126,
KW   ECO:0000256|RuleBase:RU000485};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014071}.
FT   DOMAIN          236..533
FT                   /note="6-phosphogluconate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01350"
SQ   SEQUENCE   546 AA;  60170 MW;  2A47DFE16908807F CRC64;
     MLCFSYLRTF LKQRRLRTLF CVQCLLDDEA SVARILSVAR TRISSLAAQL TTRTMSSQAV
     ADIGLIGLAV MGQNLILNMN DKGFTVCAYN RTTSKVDDFL ANEAKGTNVV GAKSIEEFVA
     KLKRPRKMIL LVKAGPAVDA FIQQLLPHLE EGDIVIDGGN SHYPDSIRRC KELEAKGILF
     VGSGVSGGEE GARHGPSLMP GGSDAAWPHI KEIFQKTAAQ SDGEPCCDWV GQTGAGHYVK
     MVHNGIEYGD MQLICEAYDI LKHGLGLAES EIGDIFTKWN TGVLDSFLIE ITRDILKYND
     EDGTPLLTKI MDSAGQKGTG KWTAINALDL GQPVTLIGEA VFARCLSSLK GERTRASKIL
     GGPQIKPFEG NKEQFIADLE QALYASKIVS YAQGFMLMRE AAKEYDWKLN NPSIALMWRG
     GCIIRSVFLK DITAAFRKNP ELENLLFDDF FNKAIHQAQE GWRRVVAQAI LWGIPTPAFS
     TALAFFDGYR REQLPANLLQ AQRDYFGAHT FRILPQYASA KLPEGQDIHI NWTGRGGNVS
     ASTYQA
//
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