ID A0A0C3Q7U6_9AGAM Unreviewed; 490 AA.
AC A0A0C3Q7U6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485};
DE EC=1.1.1.44 {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485};
GN ORFNames=M407DRAFT_24904 {ECO:0000313|EMBL:KIO25745.1};
OS Tulasnella calospora MUT 4182.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Tulasnellaceae; Tulasnella.
OX NCBI_TaxID=1051891 {ECO:0000313|EMBL:KIO25745.1, ECO:0000313|Proteomes:UP000054248};
RN [1] {ECO:0000313|EMBL:KIO25745.1, ECO:0000313|Proteomes:UP000054248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUT 4182 {ECO:0000313|EMBL:KIO25745.1,
RC ECO:0000313|Proteomes:UP000054248};
RG DOE Joint Genome Institute;
RA Kuo A., Girlanda M., Perotto S., Kohler A., Nagy L.G., Floudas D.,
RA Copeland A., Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K.,
RA Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C., Sun H.,
RA Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA Nordberg H.P., Cantor M.N., Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUT 4182 {ECO:0000313|Proteomes:UP000054248};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) 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 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|PIRNR:PIRNR000109,
CC ECO:0000256|RuleBase:RU000485}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|PIRNR:PIRNR000109}.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008419, ECO:0000256|PIRNR:PIRNR000109,
CC ECO:0000256|RuleBase:RU000485}.
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DR EMBL; KN823036; KIO25745.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3Q7U6; -.
DR STRING; 1051891.A0A0C3Q7U6; -.
DR HOGENOM; CLU_024540_4_2_1; -.
DR OrthoDB; 3013545at2759; -.
DR UniPathway; UPA00115; UER00410.
DR Proteomes; UP000054248; 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 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.
DR PROSITE; PS00461; 6PGD; 1.
PE 3: Inferred from homology;
KW Gluconate utilization {ECO:0000256|ARBA:ARBA00023064,
KW ECO:0000256|RuleBase:RU000485};
KW NADP {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000109,
KW ECO:0000256|RuleBase:RU000485};
KW Pentose shunt {ECO:0000256|ARBA:ARBA00023126,
KW ECO:0000256|PIRNR:PIRNR000109};
KW Reference proteome {ECO:0000313|Proteomes:UP000054248}.
FT DOMAIN 181..477
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01350"
FT ACT_SITE 185
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-1"
FT ACT_SITE 192
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-1"
FT BINDING 12..17
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT BINDING 35..37
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT BINDING 77..79
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT BINDING 105
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT BINDING 105
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT BINDING 131..133
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT BINDING 188..189
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT BINDING 193
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT BINDING 262
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT BINDING 289
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT BINDING 447
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT BINDING 453
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
SQ SEQUENCE 490 AA; 53378 MW; 2394399D5076798E CRC64;
MSEAVADIGL IGLAVMGQNL ILNMNDKGFT VCAYNRTTSK VDDFLANEAK GTNVVGAHSV
DELISKLKKP RRIILLVKAG PAVDAFIDQL APKLEKGDII IDGGNSHYPD SIRRCKALEE
KGLLFVGSGV SGGEEGARNG PSLMPGGSAA AWPHIKEIFQ KTAAQAYDEP CCDWVGETGS
GHYVKMVHNG IEYGDMQLIA EAYDILKRGL GLSEDEIAAI FDKWNKGVLD SFLIDITANI
LKFKDEDGVA MVNKILDSAG QKGTGKWTAV AALDAGMPVT LIGEAVFARC LSSIKGERER
ASKVLSGPQK EPFRGDKQQF IDDLEQALYA SKLISYTQGF LLMRETAKEM NWNLNYGAIA
RMWRGGCIIK SVFLNDISNA YKNTKVESLL FDDFFNKAIH TAQPGWRRVI AQAVLWGVPT
PAFSTALAFF DGYRSEIVPA NIIQAQRDYF GAHTFKVLPG KENDKLKPGV DIHINWTGRG
GNVSASTYNA
//
