ID   DHE4_NEUCR              Reviewed;         454 AA.
AC   P00369; Q7RVE1;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 154.
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=gdh; Synonyms=am; ORFNames=18F11.230, NCU01195;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6231215; DOI=10.1016/0378-1119(83)90195-6;
RA   Kinnaird J.H., Fincham J.R.S.;
RT   "The complete nucleotide sequence of the Neurospora crassa am (NADP-
RT   specific glutamate dehydrogenase) gene.";
RL   Gene 26:253-260(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-454, AND ACETYLATION AT SER-2.
RX   PubMed=1002; DOI=10.1042/bj1490757;
RA   Holder A.A., Wootton J.C., Baron A.J., Chambers G.K., Fincham J.R.S.;
RT   "The amino acid sequence of Neurospora NADP-specific glutamate
RT   dehydrogenase. Peptic and chymotryptic peptides and the complete
RT   sequence.";
RL   Biochem. J. 149:757-773(1975).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
RX   PubMed=6299898; DOI=10.1016/0378-1119(82)90207-4;
RA   Kinnaird J.H., Keighren M.A., Kinsey J.A., Eaton M., Fincham J.R.S.;
RT   "Cloning of the am (glutamate dehydrogenase) gene of Neurospora crassa
RT   through the use of a synthetic DNA probe.";
RL   Gene 20:387-396(1982).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
RX   PubMed=6325296; DOI=10.1016/0378-1119(84)90242-7;
RA   Rambosek J.A., Kinsey J.A.;
RT   "An unstable mutant gene of the am locus of Neurospora results from a small
RT   duplication.";
RL   Gene 27:101-107(1984).
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; K01409; AAA33558.1; -; Genomic_DNA.
DR   EMBL; AL670011; CAD21426.1; -; Genomic_DNA.
DR   EMBL; CM002240; EAA32325.1; -; Genomic_DNA.
DR   EMBL; K01653; AAA33557.1; -; Genomic_DNA.
DR   EMBL; K02468; AAA33559.1; -; Genomic_DNA.
DR   PIR; A91506; DENCEN.
DR   RefSeq; XP_961561.1; XM_956468.3.
DR   AlphaFoldDB; P00369; -.
DR   SMR; P00369; -.
DR   STRING; 367110.P00369; -.
DR   iPTMnet; P00369; -.
DR   PaxDb; 5141-EFNCRP00000004414; -.
DR   EnsemblFungi; EAA32325; EAA32325; NCU01195.
DR   GeneID; 3877684; -.
DR   KEGG; ncr:NCU01195; -.
DR   VEuPathDB; FungiDB:NCU01195; -.
DR   HOGENOM; CLU_025763_2_0_1; -.
DR   InParanoid; P00369; -.
DR   OMA; MIMGWMM; -.
DR   OrthoDB; 45283at2759; -.
DR   BioCyc; MetaCyc:MONOMER-13461; -.
DR   Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IBA:GO_Central.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IBA:GO_Central.
DR   CDD; cd05313; NAD_bind_2_Glu_DH; 1.
DR   Gene3D; 1.10.285.10; Glutamate Dehydrogenase, chain A, domain 3; 2.
DR   Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR006095; Glu/Leu/Phe/Val/Trp_DH.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
DR   InterPro; IPR006097; Glu/Leu/Phe/Val/Trp_DH_dimer.
DR   InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR   InterPro; IPR014362; Glu_DH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR033922; NAD_bind_Glu_DH.
DR   PANTHER; PTHR43571; NADP-SPECIFIC GLUTAMATE DEHYDROGENASE 1-RELATED; 1.
DR   PANTHER; PTHR43571:SF1; NADP-SPECIFIC GLUTAMATE DEHYDROGENASE 1-RELATED; 1.
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; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; NADP; Oxidoreductase;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1002"
FT   CHAIN           2..454
FT                   /note="NADP-specific glutamate dehydrogenase"
FT                   /id="PRO_0000182790"
FT   ACT_SITE        114
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:1002"
FT   CONFLICT        57
FT                   /note="N -> D (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        314..315
FT                   /note="QN -> ED (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        451
FT                   /note="Missing (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   454 AA;  48853 MW;  908B56A63837DA28 CRC64;
     MSNLPSEPEF EQAYKELAYT LENSSLFQKH PEYRTALTVA SIPERVIQFR VVWEDDNGNV
     QVNRGYRVQF NSALGPYKGG LRLHPSVNLS ILKFLGFEQI FKNALTGLSM GGGKGGADFD
     PKGKSDAEIR RFCCAFMAEL HKHIGADTDV PAGDIGVGGR EIGYMFGAYR KAANRFEGVL
     TGKGLSWGGS LIRPEATGYG LVYYVGHMLE YSGAGSYAGK RVALSGSGNV AQYAALKLIE
     LGATVVSLSD SKGALVATGE SGITVEDINA VMAIKEARQS LTSFQHAGHL KWIEGARPWL
     HVGKVDIALP CATQNEVSKE EAEGLLAAGC KFVAEGSNMG CTLEAIEVFE NNRKEKKGEA
     VWYAPGKAAN CGGVAVSGLE MAQNSQRLNW TQAEVDEKLK DIMKNAFFNG LNTAKTYVEA
     AEGELPSLVA GSNIAGFVKV AQAMHDQGDW WSKN
//