ID B8NP68_ASPFN Unreviewed; 516 AA.
AC B8NP68;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|PIRNR:PIRNR000109};
DE EC=1.1.1.44 {ECO:0000256|PIRNR:PIRNR000109};
GN ORFNames=AFLA_128510 {ECO:0000313|EMBL:EED48628.1}, G4B84_002622
GN {ECO:0000313|EMBL:QMW27333.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED48628.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED48628.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875}, and NRRL3357
RC {ECO:0000313|EMBL:EED48628.1};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
RN [2] {ECO:0000313|EMBL:QMW27333.1, ECO:0000313|Proteomes:UP000515286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL3357 {ECO:0000313|EMBL:QMW27333.1,
RC ECO:0000313|Proteomes:UP000515286};
RA Fountain J.C., Clevenger J.P., Nadon B., Youngblood R.C., Korani W.,
RA Chang P.-K., Starr D., Wang H., Isett B., Johnston H.R., Wiggins R.,
RA Chu Y., Agarwal G., Kemerait R.C., Pandey M.K., Bhatnagar D.,
RA Ozias-Akins P., Varshney R.K., Scheffler B.E., Vaughn J.N., Guo B.;
RT "Two New Chromosome-Level Aspergillus flavus Reference Genomes Reveal a
RT Large Insertion Potentially Contributing to Isolate Stress Tolerance and
RT Aflatoxin Production.";
RL Submitted (JUL-2020) 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; EQ963481; EED48628.1; -; Genomic_DNA.
DR EMBL; CP059867; QMW27333.1; -; Genomic_DNA.
DR RefSeq; XP_002382044.1; XM_002382003.1.
DR AlphaFoldDB; B8NP68; -.
DR STRING; 332952.B8NP68; -.
DR EnsemblFungi; EED48628; EED48628; AFLA_128510.
DR VEuPathDB; FungiDB:AFLA_012670; -.
DR eggNOG; KOG2653; Eukaryota.
DR HOGENOM; CLU_024540_4_0_1; -.
DR OMA; FMFSITH; -.
DR OrthoDB; 3013545at2759; -.
DR UniPathway; UPA00115; UER00410.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR Proteomes; UP000515286; Chromosome 2.
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}.
FT DOMAIN 194..514
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01350"
FT ACT_SITE 198
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-1"
FT ACT_SITE 205
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-1"
SQ SEQUENCE 516 AA; 57304 MW; F80A280EB6425320 CRC64;
MPSEDQNQQF KRIGIVGAGN MGSMMAFAFS ELGLDVSIWD VKKENVDQLL QSAKDIKGQG
KIEGFEDIGE FTQSLEGQGE RKLFIFSITH GDPADSVLSK IKHALKKGDI ILDGGNENYR
RTERRQKECE EIGVSWIGTG VSGGYQSARR GPSLSPGGDE KALELVLPLL ERYAAKDRKT
GQPCVARVGP AGSGHFVKMV HNGIEGGMLS AVAEAWSILH YGLGLKYDEI GDIFDEWNQK
GELRNNFLLD IGADVCHRRK SPEGDGKGEG IGEKNEYVLD DVLDKVVQDD DDTEGTPYWC
VMETANRHVS APTIATGHYM RIASGNRAER LRVAEKLQMP KPKPIEGIKD RRLFIEDLRR
AVYCCFLSSF CQGLELIARA SDDEGWNIDL SKCLQIWRGG CIIQSEAIAD LLQPLLKKDV
HYTNLKDIDE VAHALKHNFD SLKRIVIDST VFDQYIPAIS ATLEYLKYAG GTMLPTKFME
AQMDLFGAHA YYKPGVPGED PGPVKKGPHH YEWRPA
//
