6PGD_CUNEL
ID 6PGD_CUNEL Reviewed; 485 AA.
AC O60037;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating;
DE EC=1.1.1.44;
GN Name=6-PGD;
OS Cunninghamella elegans.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Cunninghamella.
OX NCBI_TaxID=4853;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 36112 / DSM 8217 / PA-1;
RX PubMed=9868787; DOI=10.1111/j.1574-6968.1998.tb13346.x;
RA Wang R.F., Khan A.A., Cao W.W., Cerniglia C.E.;
RT "Identification and sequencing of a cDNA encoding 6-phosphogluconate
RT dehydrogenase from a fungus, Cunninghamella elegans and expression of the
RT gene in Escherichia coli.";
RL FEMS Microbiol. Lett. 169:397-402(1998).
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:0000250}.
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 -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 3/3.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; Y17297; CAA76734.1; -; mRNA.
DR AlphaFoldDB; O60037; -.
DR SMR; O60037; -.
DR UniPathway; UPA00115; UER00410.
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; 1.10.1040.10; -; 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 PANTHER; PTHR11811; PTHR11811; 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; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00873; gnd; 1.
DR PROSITE; PS00461; 6PGD; 1.
PE 2: Evidence at transcript level;
KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt.
FT CHAIN 1..485
FT /note="6-phosphogluconate dehydrogenase, decarboxylating"
FT /id="PRO_0000090073"
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 193
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 12..17
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 35..37
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 77..79
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 131..133
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 189..190
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 290
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 449
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 455
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
SQ SEQUENCE 485 AA; 53102 MW; F7E6DDFF3D21EFB2 CRC64;
MVEAVADIGL IGLAVMGQNL ILNMNDHGFV VCAYNRTTSK VDDFLANEAK GTNVVGAHSV
EELCAKLKRP RKVMLLVKAG SAVDAFIDQL LPHLEEGDII IDGGNSHFPD SIRRTKELEA
KGILFVGSGV SGGEEGARYG PSLMPGGNSK AWEHIQPIFQ AIAAKAPDGA SCCEWVGETG
AGHYVKMVHN GIEYGDMQLI TEVYQILHEG LGLSHDEMAD IFEEWNKGDL DSFLIEITRD
ILRFKDTDGQ PLVTKIRDTA GQKGTGKWTA IDSLDRGIPV TLIGEAVYSR CLSSLKDERV
RASKILQGPS SSKFTGDKKT FIAQLGQALY AAKIVSYAQG YMLMRQAAKD YEWKLNNAGI
ALMWRGGCII RSVFLGKIRD AYTKNPELEN LLFDDFFKDA TAKAQDAWRN VTAQAVLMGI
PTPALSTALN FYDGLRHEIL PANLLQAQRD YFGAHTYELL HTPGKWVHTN WTGRGGNVSA
STYDA
