DHE2_NEUCR
ID DHE2_NEUCR Reviewed; 1050 AA.
AC P00365; Q02222; Q7RUZ7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 4.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=NAD-specific glutamate dehydrogenase;
DE Short=NAD-GDH;
DE EC=1.4.1.2;
GN Name=gdh-1; ORFNames=NCU00461;
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=8398079; DOI=10.1139/o93-032;
RA Kapoor M., Vijayaraghavan Y., Kadonaga R., LaRue K.E.;
RT "NAD(+)-specific glutamate dehydrogenase of Neurospora crassa: cloning,
RT complete nucleotide sequence, and gene mapping.";
RL Biochem. Cell Biol. 71:205-219(1993).
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=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 [3]
RP PROTEIN SEQUENCE OF 1-44 AND 47-353.
RX PubMed=6447150; DOI=10.1016/s0021-9258(19)43930-6;
RA Haberland M.E., Smith E.L.;
RT "Nicotinamide adenine dinucleotide-specific glutamate dehydrogenase of
RT Neurospora crassa. Isolation and sequences of several cyanogen bromide
RT peptides from the NH2-terminal portion of the peptide chain.";
RL J. Biol. Chem. 255:7984-7992(1980).
RN [4]
RP PROTEIN SEQUENCE OF 381-1050.
RX PubMed=21191; DOI=10.1016/s0021-9258(17)40950-1;
RA Austen B.M., Haberland M.E., Nyc J.F., Smith E.L.;
RT "Nicotinamide adenine dinucleotide-specific glutamate dehydrogenase of
RT Neurospora. IV. The COOH-terminal 669 residues of the peptide chain;
RT comparison with other glutamate dehydrogenases.";
RL J. Biol. Chem. 252:8142-8149(1977).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 642-948.
RX PubMed=2521336; DOI=10.1016/s0021-9258(19)85060-3;
RA Vierula P.J., Kapoor M.;
RT "NAD-specific glutamate dehydrogenase of Neurospora crassa. cDNA cloning
RT and gene expression during derepression.";
RL J. Biol. Chem. 264:1108-1114(1989).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH +
CC NH4(+); Xref=Rhea:RHEA:15133, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.2;
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA27544.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; S66039; AAB28355.1; -; Genomic_DNA.
DR EMBL; CM002238; EAA27544.2; ALT_INIT; Genomic_DNA.
DR EMBL; M23436; AAA33601.1; -; mRNA.
DR PIR; A92284; DENCED.
DR PIR; T46599; T46599.
DR RefSeq; XP_956780.2; XM_951687.3.
DR AlphaFoldDB; P00365; -.
DR STRING; 5141.EFNCRP00000000364; -.
DR EnsemblFungi; EAA27544; EAA27544; NCU00461.
DR GeneID; 3872927; -.
DR KEGG; ncr:NCU00461; -.
DR HOGENOM; CLU_005220_0_0_1; -.
DR InParanoid; P00365; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central.
DR GO; GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IEA:InterPro.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR016210; NAD-GDH_euk.
DR Pfam; PF00208; ELFV_dehydrog; 1.
DR PIRSF; PIRSF000184; GDH_NAD; 1.
DR SMART; SM00839; ELFV_dehydrog; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..1050
FT /note="NAD-specific glutamate dehydrogenase"
FT /id="PRO_0000182732"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 594
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT CONFLICT 3..5
FT /note="SPS -> APD (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 11
FT /note="H -> R (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 31..41
FT /note="HVSYPKVNGNG -> VPYSKVDGGN (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="V -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 113..114
FT /note="TS -> ST (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="T -> TTN (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="Missing (in Ref. 1; AAB28355)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="P -> PEGDP (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 345..347
FT /note="LPQ -> PQL (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 351..352
FT /note="HN -> NH (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 461..464
FT /note="EVLS -> SEVL (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 637
FT /note="L -> V (in Ref. 1; AAB28355)"
FT /evidence="ECO:0000305"
FT CONFLICT 660
FT /note="T -> I (in Ref. 1; AAB28355)"
FT /evidence="ECO:0000305"
FT CONFLICT 708..709
FT /note="Missing (in Ref. 1; AAB28355)"
FT /evidence="ECO:0000305"
FT CONFLICT 753
FT /note="N -> D (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 788
FT /note="D -> N (in Ref. 5; AAA33601)"
FT /evidence="ECO:0000305"
FT CONFLICT 799..801
FT /note="VVH -> HV (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 845..846
FT /note="ST -> TS (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 909
FT /note="D -> N (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1024
FT /note="V -> VE (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1035
FT /note="Missing (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1038..1039
FT /note="DF -> AD (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1041
FT /note="S -> T (in Ref. 1; AAB28355)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1050 AA; 118584 MW; CDCACCFD221D2CB3 CRC64;
MDSPSAPVPA HKLVDRLKDQ TPRHPSPQPT HVSYPKVNGN GHRVLRSATV GYVAPVFQGK
AEQMKQVKNI IVQGGWIPET LVDGQIAWFY NELGIDDVYF QLENPQAVAN HITSLYAAKV
AAFSREDKRE EIRLDMEASD HAIYIDTSEP GMTSFDGPRY EHRLESKYLD GDDTSKRFRV
ETFRSPGVLG QKENSKAALR CYFVYQCLFV DSNADPKETR LEVISDRMFL AKATKNTKQI
YQDIIQVAVS RHGPVIEVFD IEGSEEMRLV VAFRSRTAKG IFSALSDLYH YYGVTSSRKY
VEQFSNGITV MSIYLRPAAN IDGKHPPLEQ SIHQITKEIS LLYCLPQNKF HNMFASGELS
LQETIYAHCV WVFVQHFLNR LGTEYTSLIA ALDPKNNSHV EILSKMKKRL RTETFTPDYI
LEIISSHPQL VRALYASFAS VHLRVGSDYD RHLIAPTPVM EVLSDARLKE KITKDVSNEH
EEMVMTAFRV FNNAVLKTNF FTPTKVALSF RLNPSFLPEV EYPKPLYGMF LVITSESRGF
HLRFKDIARG GIRIVKSRSK EAYQINARNL FDENYGLAST QQRKNKDIPE GGSKGVILLD
PKQQDRHREA FEKYIDSILD LLLKAETPGI KNPIVDLYGK EEILFMGPDE NTADLVDWAT
EHARARGAPW WKSFFTGKSP RLGGIPHDSY GMTTLSVREY VKGIYRKLEL DPSKIRKMQT
GGPDGDLGSN EILLSNETYT AIVDGSGVLC DPNGIDKDEL RRLAKARAMI SNFDIAKLSK
DGYRVLCDDT NVTLPNGEVV HNGTAFRNTY HLRDNGITDM FVPCGGRPES IDLSSVNKLI
KDGKSTIPYI VEGANLFITQ DAKLRLEEAG CIVYKDASAN KGGVTSSSLE VLASLSFDDK
GFVTHMCHDS RGNAPEFYQA YVKEVQNKIQ DNARLEFEAI WREHEQTGLP RSVLSDKLSL
AITSLDEDLQ RSELWDNEKI RRSVLADALP NLLINKIGLD TIIERVPDSY LRAIFGSYLA
SRFVYEFGSS PSQFAFYDFM SKRMGNINKE
