DHE4_EMENI
ID DHE4_EMENI Reviewed; 459 AA.
AC P18819; C8V8W7; Q5B504;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=NADP-specific glutamate dehydrogenase;
DE Short=NADP-GDH;
DE EC=1.4.1.4;
DE AltName: Full=NADP-dependent glutamate dehydrogenase;
GN Name=gdhA; ORFNames=AN4376;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2550758; DOI=10.1007/bf00330572;
RA Hawkins A.R., Gurr S.J., Montague P., Kinghorn J.R.;
RT "Nucleotide sequence and regulation of expression of the Aspergillus
RT nidulans gdhA gene encoding NADP dependent glutamate dehydrogenase.";
RL Mol. Gen. Genet. 218:105-111(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH +
CC NH4(+); Xref=Rhea:RHEA:11612, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.4.1.4;
CC -!- SUBUNIT: Homohexamer.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000305}.
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DR EMBL; X16121; CAA34252.1; -; Genomic_DNA.
DR EMBL; AACD01000076; EAA60293.1; -; Genomic_DNA.
DR EMBL; BN001303; CBF77653.1; -; Genomic_DNA.
DR PIR; S04904; S04904.
DR RefSeq; XP_661980.1; XM_656888.1.
DR AlphaFoldDB; P18819; -.
DR SMR; P18819; -.
DR STRING; 162425.CADANIAP00006082; -.
DR PRIDE; P18819; -.
DR EnsemblFungi; CBF77653; CBF77653; ANIA_04376.
DR EnsemblFungi; EAA60293; EAA60293; AN4376.2.
DR GeneID; 2872176; -.
DR KEGG; ani:AN4376.2; -.
DR VEuPathDB; FungiDB:AN4376; -.
DR eggNOG; KOG2250; Eukaryota.
DR HOGENOM; CLU_025763_2_1_1; -.
DR InParanoid; P18819; -.
DR OMA; PCFAAFP; -.
DR OrthoDB; 692851at2759; -.
DR BRENDA; 1.4.1.4; 517.
DR Proteomes; UP000000560; Chromosome III.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IDA:AspGD.
DR GO; GO:0005576; C:extracellular region; IDA:AspGD.
DR GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IMP:AspGD.
DR GO; GO:0097308; P:cellular response to farnesol; IEP:AspGD.
DR GO; GO:0006537; P:glutamate biosynthetic process; IBA:GO_Central.
DR CDD; cd05313; NAD_bind_2_Glu_DH; 1.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
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 SUPFAM; SSF53223; SSF53223; 1.
DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE 3: Inferred from homology;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..459
FT /note="NADP-specific glutamate dehydrogenase"
FT /id="PRO_0000182785"
FT ACT_SITE 114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT CONFLICT 206
FT /note="E -> Q (in Ref. 1; CAA34252)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 459 AA; 49609 MW; 6825E0399C056F7D CRC64;
MSNLPVEPEF EQAYKELAST LENSTLFEQH PEYRRALQVV SVPERVIQFR VVWENDKGEV
QINRGYRVQF NSALGPYKGG LRFHPSVNLS ILKFLGFEQI FKNALTGLNM GGGKGGSDFD
PKGKSDSEIR RFCTAFMTEL CKHIGADTDV PAGDIGVTGR EVGFLFGQYR RIRNQWEGVL
TGKGGSWGGS LIRPEATGYG VVYYVEHMIK HVTGGKESFA GKRVAISGSG NVAQYAALKV
IELGGSVVSL SDSKGSLIVK DESASFTPEE IALIADLKVA RKQLSELATS SAFAGKFTYI
PDARPWTNIP GKFEVALPSA TQNEVSGEEA EHLIKSGVRY IAEGSNMGCT QAAIDIFEAH
RNANPGDAIW YAPGKAANAG GVAVSGLEMA QNSARLSWTS EEVDARLKGI MEDCFKNGLE
TAQKFATPAK GVLPSLVTGS NIAGFTKVAE AMKDQGDWW