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Database: UniProt
Entry: W2SCQ5_9EURO
LinkDB: W2SCQ5_9EURO
Original site: W2SCQ5_9EURO 
ID   W2SCQ5_9EURO            Unreviewed;       484 AA.
AC   W2SCQ5;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|PIRNR:PIRNR000109};
DE            EC=1.1.1.44 {ECO:0000256|PIRNR:PIRNR000109};
GN   ORFNames=HMPREF1541_09646 {ECO:0000313|EMBL:ETN45813.1};
OS   Cyphellophora europaea CBS 101466.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX   NCBI_TaxID=1220924 {ECO:0000313|EMBL:ETN45813.1, ECO:0000313|Proteomes:UP000030752};
RN   [1] {ECO:0000313|EMBL:ETN45813.1, ECO:0000313|Proteomes:UP000030752}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101466 {ECO:0000313|EMBL:ETN45813.1,
RC   ECO:0000313|Proteomes:UP000030752};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Phialophora europaea CBS 101466.";
RL   Submitted (MAR-2013) 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       ECO:0000256|PIRNR:PIRNR000109}.
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|PIRNR:PIRNR000109};
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|PIRNR:PIRNR000109}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR000109}.
CC   -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00008419, ECO:0000256|PIRNR:PIRNR000109}.
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DR   EMBL; KB822712; ETN45813.1; -; Genomic_DNA.
DR   RefSeq; XP_008712541.1; XM_008714319.1.
DR   AlphaFoldDB; W2SCQ5; -.
DR   STRING; 1220924.W2SCQ5; -.
DR   GeneID; 19976985; -.
DR   VEuPathDB; FungiDB:HMPREF1541_09646; -.
DR   eggNOG; KOG2653; Eukaryota.
DR   HOGENOM; CLU_024540_4_0_1; -.
DR   InParanoid; W2SCQ5; -.
DR   OrthoDB; 3013545at2759; -.
DR   UniPathway; UPA00115; UER00410.
DR   Proteomes; UP000030752; 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; 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; 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   PIRSF; PIRSF000109; 6PGD; 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   NADP {ECO:0000256|PIRNR:PIRNR000109};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000109};
KW   Pentose shunt {ECO:0000256|ARBA:ARBA00023126,
KW   ECO:0000256|PIRNR:PIRNR000109};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030752}.
FT   DOMAIN          176..482
FT                   /note="6-phosphogluconate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01350"
FT   ACT_SITE        180
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-1"
FT   ACT_SITE        187
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-1"
SQ   SEQUENCE   484 AA;  53686 MW;  397481F47ABB4227 CRC64;
     MIGCGSMGGG MALLFAEHDI TVYLEDPSEE QVDSVIQSAK KDGIGHRVEK TQDYQEMCQK
     LDSPRVFVFS LPHGNVGDSV VDGLQRYLDI GDIIIDASNE NWQNTQRRQG KLAAQGVCYI
     GMGVSGGYQA ARRGPSMCPG GDQPALKQVM PLLEKVCAKD SKGRPCVGNV GTGGCGHYVK
     MIHNGIEQAM MSAVAEAFQV MNVGLGMTLD EISEAFARWN TEGELRNTFL VSIAADICKT
     RDESGKLVLP AIQDKVVQDT DDTEGTGIWT NIEAIRLHIP VPSIATAHFL RLASGDRAQR
     VHAKETSKHH ETIHKIDQDR KEFLEDLRLA LYGACVASYV QGLKIIDKAD KENNWHINFL
     TVTQIWRAGC IIQADTITDL MEEVYTSNGT DKERNPLFSR SFMDELNKTY LPLRRVVARC
     VETNAVIPSF SATLEYMKYS SNTQLPTDFY EAELDYFGKH MFDLKSDPPG KPVTGTHHFE
     WKPA
//
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