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Database: UniProt
Entry: B6GYV9_PENRW
LinkDB: B6GYV9_PENRW
Original site: B6GYV9_PENRW 
ID   B6GYV9_PENRW            Unreviewed;       512 AA.
AC   B6GYV9;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   24-JAN-2024, entry version 88.
DE   RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|PIRNR:PIRNR000109};
DE            EC=1.1.1.44 {ECO:0000256|PIRNR:PIRNR000109};
GN   ORFNames=Pc12g08920 {ECO:0000313|EMBL:CAP80519.1}, PCH_Pc12g08920
GN   {ECO:0000313|EMBL:CAP80519.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP80519.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP80519.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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|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; AM920427; CAP80519.1; -; Genomic_DNA.
DR   RefSeq; XP_002557720.1; XM_002557674.1.
DR   AlphaFoldDB; B6GYV9; -.
DR   STRING; 500485.B6GYV9; -.
DR   GeneID; 8310626; -.
DR   KEGG; pcs:Pc12g08920; -.
DR   VEuPathDB; FungiDB:PCH_Pc12g08920; -.
DR   eggNOG; KOG2653; Eukaryota.
DR   HOGENOM; CLU_024540_4_0_1; -.
DR   OMA; FMFSITH; -.
DR   OrthoDB; 3013545at2759; -.
DR   BioCyc; PCHR:PC12G08920-MONOMER; -.
DR   UniPathway; UPA00115; UER00410.
DR   Proteomes; UP000000724; Contig Pc00c12.
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:SF68; 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:UP000000724}.
FT   DOMAIN          190..510
FT                   /note="6-phosphogluconate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01350"
FT   ACT_SITE        194
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-1"
FT   ACT_SITE        201
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-1"
SQ   SEQUENCE   512 AA;  56511 MW;  13D73818F077F9B2 CRC64;
     MTTAIKSIGV VGAGNMGSMM TLRFAELGLQ VSVWDVVKKN VDDAVNYAKQ DEAITGRVQG
     FYDINKFTKS LEGKSERKVF MFSITHGHPA DEVLRMIKPD LKAGDIVLDG GNENYRNTER
     RQRECEEIGV SWIGMGVSGG YQSARRGPSL SPGGDAKALE LVMPFLESYA AHDPKTGTAC
     VKRMGPGGSG HYIKMVHNGI EGGMLSSLAE TWQYMHEGLA MEHGEIGDVF NKWSESGELR
     GNYLVNIGAD MLHKKRTPHG DRKGEGSSRD NGYVIDDVLD KVVQDDDNTE GTPYWCLMES
     AARHVSCPTL AAAHYLRVAS GNRIERARVA KKMEMPMPKP IEGTRDHAVI IENLRQAVFC
     SFLASFCQGL ELISRASKDE GWDVNLGDCL QIWRAGCIIK SDYIADLLQP ALAGNNELTN
     AKFVDAVSHE LRQKFHSLKQ IVMEGTMFDQ YIPALSATLE YLKYEGGLGL PTQFMEAQMD
     YFGSHSYNKP GIPGEDPGPV HKGPHHYEWL PA
//
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