ID A0A2N6NC89_BEABA Unreviewed; 1061 AA.
AC A0A2N6NC89;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000184};
DE EC=1.4.1.2 {ECO:0000256|PIRNR:PIRNR000184};
GN Name=gdh-1 {ECO:0000313|EMBL:PMB64891.1};
GN ORFNames=BM221_009078 {ECO:0000313|EMBL:PMB64891.1};
OS Beauveria bassiana (White muscardine disease fungus) (Tritirachium
OS shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=176275 {ECO:0000313|EMBL:PMB64891.1, ECO:0000313|Proteomes:UP000235728};
RN [1] {ECO:0000313|EMBL:PMB64891.1, ECO:0000313|Proteomes:UP000235728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEF-007 {ECO:0000313|EMBL:PMB64891.1,
RC ECO:0000313|Proteomes:UP000235728};
RX PubMed=27470140; DOI=10.1007/s00253-016-7734-y;
RA Kim S., Lee S.J., Nai Y.S., Yu J.S., Lee M.R., Yang Y.T., Kim J.S.;
RT "Characterization of T-DNA insertion mutants with decreased virulence in
RT the entomopathogenic fungus Beauveria bassiana JEF-007.";
RL Appl. Microbiol. Biotechnol. 100:8889-8900(2016).
CC -!- FUNCTION: NAD(+)-dependent glutamate dehydrogenase which degrades
CC glutamate to ammonia and alpha-ketoglutarate.
CC {ECO:0000256|PIRNR:PIRNR000184}.
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 Evidence={ECO:0000256|PIRNR:PIRNR000184};
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|PIRNR:PIRNR000184}.
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:PMB64891.1}.
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; MRVG01000011; PMB64891.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N6NC89; -.
DR OMA; LYCLPQN; -.
DR Proteomes; UP000235728; Unassembled WGS sequence.
DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
DR InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR016210; NAD-GDH_euk.
DR PANTHER; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11606:SF42; NAD-SPECIFIC GLUTAMATE DEHYDROGENASE; 1.
DR Pfam; PF00208; ELFV_dehydrog; 1.
DR PIRSF; PIRSF000184; GDH_NAD; 1.
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 3: Inferred from homology;
KW NAD {ECO:0000256|PIRNR:PIRNR000184};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000184};
KW Reference proteome {ECO:0000313|Proteomes:UP000235728}.
FT DOMAIN 678..943
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT REGION 12..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1061 AA; 119330 MW; E72923B43FD9296A CRC64;
MSTSANKVLA NLASSESSRL PSPQPTHMSS HNSTGHRKLR SATVGYVAPE FTGKVEQMKT
VRNLILGNGW IPEALVDDQI RWFYEQLGID DVYFRIESPE VIGNQITSLY AAKVAANSRE
DKREEIRLDM EAEDHAIYID TSEPGQSNVS GPRYEVRLEA KYLDHSDRTK YRVETFRSPA
AIGASPNSKA TLRCYFVYKC DFKQSVENTD PKETNIELIS DAGFWQKATE NTKQIYQEII
QLAVSRTGPV IDIFDIEDSV EKRLVVAFRT RTARGMFSSL SDLYHYYGVT SSRKYVEQFS
NGITVMSIYL RPASTDGGYF PPMEESIHQI TKEISLLYCL PQNKFHNLFA TGALSLQEAV
YAHATWVFVQ HFLNRLGPEY VSLSEIINHN DSAQAALLSK LKRRLRTETF TPDYIYEIIQ
SHPELVRSLY ASFANVHLSV GPYERHYLAP TPKVEVLSDE RLKDRISKTV ANEHEEMVMT
AFRVFNNAIL KTNYFTPTKV ALSFRLDPSF LPMAEYPRRL YGMFLVIGAE SRGFHLRFRE
ISRGGIRIVK SRSKEAYGIN VRNLFDENYG LASTQQRKNK DIPEGGSKGV ILLDPKQQDR
AQEAFEKYID SILDLLLPAE TPGIKNPVVD LYGKQEILFM GPDENTAGLV DWATEHARTR
GAPWWKSFFT GKSPKLGGIP HDKYGMTTLS VREYVKGIYR KLNLDPSTVR KMQTGGPDGD
LGSNEILLGN EKWTAIVDGS GVLADPNGLD KDELVRLAKK RAMIGEYDMS KVSKDGYRVL
CEDNNVTLPN GEVVANGTSF RNTYHLRDTG MTDAFVPCGG RPESIDLISV NRLIKDGKSV
IPYIVEGANL FITQDAKLRL EAAGCILYKD ASANKGGVTS SSLEVLASLS FDDAGFVENM
CVDAKTGEAP QFYKDYVRSV QAKIQENAAL EFEAIWREHE KTGEPRSILS DKLSIAITDL
DEQLQKSDLW ANETIRYGIL KDALPKLLLD KIGLETIVQR VPESYLRSIF GSYLASRFVY
EFGAEPSQFA FFDFMSKRMA AINGDNGNGT ERLRRASISK H
//
