ID A0A2J6QQ68_9HELO Unreviewed; 1050 AA.
AC A0A2J6QQ68;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000184};
DE EC=1.4.1.2 {ECO:0000256|PIRNR:PIRNR000184};
GN ORFNames=NA56DRAFT_13378 {ECO:0000313|EMBL:PMD28404.1};
OS Hyaloscypha hepaticicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD28404.1, ECO:0000313|Proteomes:UP000235672};
RN [1] {ECO:0000313|EMBL:PMD28404.1, ECO:0000313|Proteomes:UP000235672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD28404.1,
RC ECO:0000313|Proteomes:UP000235672};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KZ613464; PMD28404.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6QQ68; -.
DR STRING; 1745343.A0A2J6QQ68; -.
DR OrthoDB; 89313at2759; -.
DR Proteomes; UP000235672; 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; 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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRNR:PIRNR000184};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000184};
KW Reference proteome {ECO:0000313|Proteomes:UP000235672}.
FT DOMAIN 687..951
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
SQ SEQUENCE 1050 AA; 117861 MW; 0B92B722B28E9288 CRC64;
MASLEVPTSP TINKLVKDVV AAPDRRPSPQ PAHFSVPYKN GNGNGHRVLR SATVGYIAPE
FKGKKAQMLQ GKIEEAAWIP GPLIDEQINW FYNELGIDDV YFQLENVDAI VSHVTSLYAA
KIAAFARSDK KEAIRLDMEA VDHAIYIDTS EPGVSNISGP RYEHRLEKKY LDASTDSQSY
RVETFRSPTN LSGTTPSKMT MRCYFVYQCM FVDPNPGPTE TRLEFIADRM FLAKATKNTK
QIYREIIELA VSRTGPVIEV FDIEGSKEKR LVVAFRRRTA AGLFSALSDL YHYYGVTSSR
KYVEQFSNGI TVICLYLKPA KNLESKNFPP LAASIHQITK EISLLYCIPQ NKFQALFAAG
RLSLQETIYG HCLGIFVQHF LNRLGSDYAS LVSALDKDSS AHVEILSKIK RRLRTETFTA
GYILEIIESY PELVRILYAQ FAHTHLTLGP GYTEDWVAPT PSAEVLSDTQ IGDLITRTVN
NEHEEMVMNA FRIFNNSLLK TNFYTPTKVA LSFRLRPDFL PEIEYPQPLY GMFLVISSES
RGFHLRFRDI ARGGIRIVKS RNKEAYSINA RSMFDENYGL ANTQQRKNKD IPEGGSKGVI
LLDAAHQNKG SVAFEKYIDS IMDLLLPAET PGIKNPIVDR YGKQEILFMG PDENTADLVD
WATEHARKRG APWWKSFFTG KSPKLGGIPH DAYGMTTLSV REFVKGIYRK LELDPSKVRK
MQTGGPDGDL GSNEILLSNE KYTSIVDGSG VLVDPNGIDQ NELVRLAKSR VMVSHFNMRK
LSKDGYRVLV DENNVKLPSG EVVNNGTQFR NTFHLRDTGL TDSFVPCGGR PESIDLSNVG
KLIKRGKTTI PYIVEGANLF ITQDAKLRLE AAGCILFKDA SANKGGVTSS SLEVLASLSF
DDEGFVQNMC VGADGNPPEF YKAYVKAVQE KIKSNARLEF EAIWREHKET KIPRSTLSDT
LSVAITKLDE ELQKTDLWKN EKLRRSVLAD ALPKLLIDKI GLDLIIERVP DNYLRAIFGS
YLASRFVYEF GSQPSQFAFF DFMSKRMASV
//
