(data stored in ACNUC7421 zone)

SWISSPROT: Q4WNQ8_ASPFU

ID   Q4WNQ8_ASPFU            Unreviewed;       458 AA.
AC   Q4WNQ8;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 93.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN   ORFNames=AFUA_4G06620 {ECO:0000313|EMBL:EAL90126.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL90126.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL90126.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000256|PIRNR:PIRNR000185, ECO:0000256|RuleBase:RU004417}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAL90126.1}.
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DR   EMBL; AAHF01000005; EAL90126.1; -; Genomic_DNA.
DR   RefSeq; XP_752164.1; XM_747071.1.
DR   STRING; 746128.CADAFUBP00006196; -.
DR   SwissPalm; Q4WNQ8; -.
DR   PRIDE; Q4WNQ8; -.
DR   EnsemblFungi; EAL90126; EAL90126; AFUA_4G06620.
DR   GeneID; 3509256; -.
DR   KEGG; afm:AFUA_4G06620; -.
DR   EuPathDB; FungiDB:Afu4g06620; -.
DR   HOGENOM; HOG000243799; -.
DR   InParanoid; Q4WNQ8; -.
DR   KO; K00262; -.
DR   OMA; HEPEFIQ; -.
DR   OrthoDB; 692851at2759; -.
DR   Proteomes; UP000002530; Chromosome 4.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IBA:GO_Central.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IBA:GO_Central.
DR   CDD; cd05313; NAD_bind_2_Glu_DH; 1.
DR   InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
DR   InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
DR   InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom.
DR   InterPro; IPR014362; Glu_DH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR033922; NAD_bind_Glu_DH.
DR   Pfam; PF00208; ELFV_dehydrog; 1.
DR   Pfam; PF02812; ELFV_dehydrog_N; 1.
DR   PIRSF; PIRSF000185; Glu_DH; 1.
DR   PRINTS; PR00082; GLFDHDRGNASE.
DR   SMART; SM00839; ELFV_dehydrog; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4WNQ8.
DR   SWISS-2DPAGE; Q4WNQ8.
KW   NAD {ECO:0000256|PIRSR:PIRSR000185-2};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000185-2};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000185,
KW   ECO:0000256|RuleBase:RU004417, ECO:0000313|EMBL:EAL90126.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530}.
FT   DOMAIN          190..455
FT                   /note="ELFV_dehydrog"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        114
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT   BINDING         78
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         99
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         102
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         153
FT                   /note="Substrate; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         197
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         231
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         384
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   SITE            154
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ   SEQUENCE   458 AA;  49368 MW;  D462BF2942CBAE35 CRC64;
     MSNLPHEPEF EQAYKELAST LENSTLFEKN PEYRKALAVV SVPERVVQFR VVWEDDNHQV
     QINRGYRVQF NSALGPYKGG LRFHPSVNLS ILKFLGFEQI FKNALTGLNM GGGKGGSDFD
     PKGKSDNEIR RFCVAFMTEL CKHIGADTDV PAGDIGVTGR EIGFLFGQYR KIRNQWEGVL
     TGKGGSWGGS LIRPEATGYG LVYYVDHMIK YVTKGAESFA GKRVAISGSG NVAQFAALKV
     IELGGSVVSL SDSKGSLVVN GEGSFTPAEI DIIAQLKVDR KQLSEVATTE AFATKFKYIE
     GARPWVHVGK VDVALPSATQ NEVSGEEAQA LIDAGCKFIA EGSNMGCTQA AIDIFEAHRQ
     ANPGAAAIWY APGKAANAGG VAVSGLEMAQ NSARISWTAE EVDSRLKDIM ESCFRNGLDT
     AVKYATPAEG VLPSLVTGSN IAGFTKVAEA MKEQGDWW
//

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