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Database: UniProt
Entry: A0A0D2X8S0_FUSO4
LinkDB: A0A0D2X8S0_FUSO4
Original site: A0A0D2X8S0_FUSO4 
ID   A0A0D2X8S0_FUSO4        Unreviewed;       492 AA.
AC   A0A0D2X8S0;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   22-NOV-2017, entry version 24.
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=FOXG_00279 {ECO:0000313|EMBL:KNA94058.1};
OS   Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC
OS   9935 / NRRL 34936) (Fusarium vascular wilt of tomato).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
OC   Fusarium; Fusarium oxysporum species complex.
OX   NCBI_TaxID=426428 {ECO:0000313|EnsemblFungi:FOXG_00279P0, ECO:0000313|Proteomes:UP000009097};
RN   [1] {ECO:0000313|EMBL:KNA94058.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=4287 {ECO:0000313|EMBL:KNA94058.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Ma L.-J.,
RA   Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E., Brockman W., MacCallum I.A., Young S., LaButti K.,
RA   DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P.,
RA   Pearson M., Howarth C., Larson L., White J., O'Leary S., Kodira C.,
RA   Zeng Q., Yandava C., Alvarado L., Kistler C., Shim W.-B., Kang S.,
RA   Woloshuk C.;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KNA94058.1, ECO:0000313|EnsemblFungi:FOXG_00279P0, ECO:0000313|Proteomes:UP000009097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4287 {ECO:0000313|EMBL:KNA94058.1}, and 4287 / CBS 123668 /
RC   FGSC 9935 / NRRL 34936 {ECO:0000313|EnsemblFungi:FOXG_00279P0,
RC   ECO:0000313|Proteomes:UP000009097};
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J.,
RA   Daboussi M.-J., Di Pietro A., Dufresne M., Freitag M., Grabherr M.,
RA   Henrissat B., Houterman P.M., Kang S., Shim W.-B., Woloshuk C.,
RA   Xie X., Xu J.-R., Antoniw J., Baker S.E., Bluhm B.H., Breakspear A.,
RA   Brown D.W., Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M.,
RA   Danchin E.G.J., Diener A., Gale L.R., Gardiner D.M., Goff S.,
RA   Hammond-Kosack K.E., Hilburn K., Hua-Van A., Jonkers W., Kazan K.,
RA   Kodira C.D., Koehrsen M., Kumar L., Lee Y.-H., Li L., Manners J.M.,
RA   Miranda-Saavedra D., Mukherjee M., Park G., Park J., Park S.-Y.,
RA   Proctor R.H., Regev A., Ruiz-Roldan M.C., Sain D., Sakthikumar S.,
RA   Sykes S., Schwartz D.C., Turgeon B.G., Wapinski I., Yoder O.,
RA   Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A., Kistler H.C.,
RA   Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
RN   [3] {ECO:0000313|EnsemblFungi:FOXG_00279P0}
RP   IDENTIFICATION.
RC   STRAIN=4287 / CBS 123668 / FGSC 9935 / NRRL 34936
RC   {ECO:0000313|EnsemblFungi:FOXG_00279P0};
RG   EnsemblFungi;
RL   Submitted (MAR-2015) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the oxidative decarboxylation of 6-
CC       phosphogluconate to ribulose 5-phosphate and CO(2), with
CC       concomitant reduction of NADP to NADPH.
CC       {ECO:0000256|PIRNR:PIRNR000109}.
CC   -!- CATALYTIC ACTIVITY: 6-phospho-D-gluconate + NADP(+) = D-ribulose
CC       5-phosphate + CO(2) + NADPH. {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):
CC       step 3/3. {ECO:0000256|PIRNR:PIRNR000109,
CC       ECO:0000256|RuleBase:RU000485}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR000109}.
CC   -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase
CC       family. {ECO:0000256|PIRNR:PIRNR000109,
CC       ECO:0000256|RuleBase:RU000485}.
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DR   EMBL; DS231696; KNA94058.1; -; Genomic_DNA.
DR   RefSeq; XP_018232104.1; XM_018376517.1.
DR   STRING; 5507.FOXG_00279P0; -.
DR   EnsemblFungi; FOXG_00279T0; FOXG_00279P0; FOXG_00279.
DR   GeneID; 28942598; -.
DR   KEGG; fox:FOXG_00279; -.
DR   KO; K00033; -.
DR   OMA; NSHYPDS; -.
DR   UniPathway; UPA00115; UER00410.
DR   Proteomes; UP000009097; Chromosome 1.
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   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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000009097};
KW   Gluconate utilization {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|PIRNR:PIRNR000109,
KW   ECO:0000256|RuleBase:RU000485};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009097}.
FT   DOMAIN      181    479       6PGD. {ECO:0000259|SMART:SM01350}.
FT   NP_BIND      12     17       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   NP_BIND      35     37       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   NP_BIND      77     79       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   REGION      131    133       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   REGION      188    189       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   ACT_SITE    185    185       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000109-1}.
FT   ACT_SITE    192    192       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000109-1}.
FT   BINDING     105    105       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   BINDING     105    105       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     193    193       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     262    262       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
FT   BINDING     289    289       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     449    449       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
FT   BINDING     455    455       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
SQ   SEQUENCE   492 AA;  54202 MW;  15EBD7330A8F2785 CRC64;
     MSGPVADLGL IGLAVMGQNL ILNMADNGFT ICAFNRTVSK VDRFLENEAK GKSIVGAKTV
     EEFVSKLKSP RRVMLLVQAG QAVDDWIEKI LPLLDAGDII IDGGNSHFPD SNRRTKYLAG
     KNIRFVGSGV SGGEEGARYG PSLMPGGNEE AWPHIKDIFQ SIAAKSDGEA CCEWVGDEGA
     GHYVKMVHNG IEYGDMQLIC EAYDIMKRGL GLSSKEIGDV FAKWNKGVLD SFLIEITRDI
     MYFNDDDGTA LVEKILDKAG QKGTGKWTAV NALDLGQPVT LIAEAVLARC LSAIKDERAT
     ASTKLEFVSR TTKFEGDKEQ FLEDLEQALY ASKIISYAQG FMLMQEAARE FNWKLNKPSI
     ALMWRGGCII RSVFLKDITH AYRSQPDLQN LLFDDFFNKA IHKAQPGWRD VVSKAALLGI
     PTPAFSTALS WFDGYRTKDL PANLLQAQRD YFGAHTFRIK PENASDKYPN GQDIHVNWTG
     RGGNVSASTY QA
//
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