GenomeNet

Database: UniProt
Entry: A0A0J9VN04_FUSO4
LinkDB: A0A0J9VN04_FUSO4
Original site: A0A0J9VN04_FUSO4 
ID   A0A0J9VN04_FUSO4        Unreviewed;       504 AA.
AC   A0A0J9VN04;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   22-NOV-2017, entry version 15.
DE   RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|PIRNR:PIRNR000109};
DE            EC=1.1.1.44 {ECO:0000256|PIRNR:PIRNR000109};
GN   ORFNames=FOXG_11985 {ECO:0000313|EMBL:KNB12373.1};
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|EMBL:KNB12373.1};
RN   [1] {ECO:0000313|EMBL:KNB12373.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=4287 {ECO:0000313|EMBL:KNB12373.1};
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:KNB12373.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4287 {ECO:0000313|EMBL:KNB12373.1};
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).
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   -!- 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   -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR000109}.
CC   -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase
CC       family. {ECO:0000256|PIRNR:PIRNR000109}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; DS231711; KNB12373.1; -; Genomic_DNA.
DR   RefSeq; XP_018250418.1; XM_018391716.1.
DR   STRING; 5507.FOXG_11985P0; -.
DR   GeneID; 28953354; -.
DR   KEGG; fox:FOXG_11985; -.
DR   KO; K00033; -.
DR   UniPathway; UPA00115; UER00410.
DR   GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
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; 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.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|PIRNR:PIRNR000109};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000109};
KW   Pentose shunt {ECO:0000256|PIRNR:PIRNR000109}.
FT   DOMAIN      189    493       6PGD. {ECO:0000259|SMART:SM01350}.
FT   ACT_SITE    193    193       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000109-1}.
FT   ACT_SITE    200    200       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000109-1}.
SQ   SEQUENCE   504 AA;  56910 MW;  36825A8C4315AB21 CRC64;
     MSERQIAKIG MVGMGSMGSM MSLLFAEKGC KVYYYDISEY NMKAAEKMVK DVNEETRVFR
     QHSYQQLCEE IYSENHPRII IFSIPHGNPG DECVKALRPY MTKGDIILDC SNEFYGNTER
     RQADLAKDSM FYVGCGVSGG YQSARAGPSM SPGGDPQALE IIMPLLRRVA AKDHDGRPCT
     CPIGPGGSGH YVKMIHNGIE QGMMSVISEV WYILTKGLQL SYEEAAGVFE QWNQTKELYN
     TFLIYIAVDI NRIKDEEGRY VLGRVQDKVV QDVDNTEGTG TWSCEEAVRL HVPAANIVSA
     HLFRCTSAEL DQRAADAEAS GRRQSSAMKV PSRDEFIEDL RKATYFCLLL CFTQGLQIIR
     EMDQQREWHI NYQDLLHVWS AGSIIQAGGI MDLLHKVYSE SPSKNNLLSN SQLEKQLTSL
     LPSMKRCIIT ALESDMVIPA MSQSLEYYKY STSVDLPTQL TEAELDYFGN HKFDLKEEHR
     GEPSKGKHHF EWKPAKGESD KSRL
//
DBGET integrated database retrieval system