ID A0A1Y1WIM1_9FUNG Unreviewed; 1034 AA.
AC A0A1Y1WIM1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, 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=DL89DRAFT_265338 {ECO:0000313|EMBL:ORX73215.1};
OS Linderina pennispora.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Kickxellomycetes; Kickxellales; Kickxellaceae; Linderina.
OX NCBI_TaxID=61395 {ECO:0000313|EMBL:ORX73215.1, ECO:0000313|Proteomes:UP000193922};
RN [1] {ECO:0000313|EMBL:ORX73215.1, ECO:0000313|Proteomes:UP000193922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12442 {ECO:0000313|EMBL:ORX73215.1,
RC ECO:0000313|Proteomes:UP000193922};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-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}.
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:ORX73215.1}.
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DR EMBL; MCFD01000002; ORX73215.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1WIM1; -.
DR STRING; 61395.A0A1Y1WIM1; -.
DR OrthoDB; 89313at2759; -.
DR Proteomes; UP000193922; 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:UP000193922}.
FT DOMAIN 666..931
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
SQ SEQUENCE 1034 AA; 116114 MW; 35B2830A33AC2526 CRC64;
MSATPVQQCD YTDNVYSGKQ DHRAQVCILV EKEGLIPKHL IDSEVGWFYD ILGIDDMYFM
LEDPAAVAGH ITALYGAQLS NSTRPGDIGI HFENRHERGA VFIHNSTPGI SKTEGPNYEK
MIDAEYLDVS VPQSAYRLES YRSRGKVSKS LDASLRAYFV NQCDFVNPDP KGDEIHDIKQ
TSDRTFLAKA TPAVLDLYSS VISKVLDRTG PVITQTTLPS GEHRLVIGYR QRSTQGYFAG
LSDLYHYYHM YSSRKYVEQF SCGVTVISLY LDTSKHAKPQ GSSPVLSAAN GTASIDDSIR
QIMKEASLVY CIPSTPFQTL FRTGVLSVQE AVYGYTCWIF AQHFLNRLGS EYATLVEILD
PSDATDMEVL AKLKKRLRQE TFTRELILDI MLRYPELLKD LYKDFASEHY IHSELPSYVG
KLADRLNDEL RVSLSEQRLQ DKAPLAKEDL LAKITRTTTN ENEAMVLRSM LDFNKHVLKT
NFYQPTKVAL SFRMDPGFLP VIEYPAKPFG IFLVVGNEFR GFHVRFQDVA RGGIRIVRSR
NPEAFSINQR TLFDENYSLA STQHRKNKDI PEGGSKGTIL LNMDSQDRPF VAFEKYVDAI
LDLLLTGQSP GIKDRLVDRL GREEILFFGP DEGTAGYMDW ASQHARKRGA PFWKAFTTGK
SQTMGGIPHD VYGMTTRSVH QYVLGIIRQL GLDESVCTKF QTGGPDGDLG SNEIKISHDR
TTAVVDGSGV LYDPRGIDRT ELTRLANERK MIQHFDVSKL SPEGFRVLVD EYQVTLPDGT
LVQDGLSFRN GFHLNKLAAA DFFVPCGGRP ESIDINNVHS LFDAEGNARF KYVVEGANLF
FTQDARLRLE KAGVHLFKDA SANKGGVTSS SLEVLAALAL TDEEHGRLMC EQPDGSLPEF
YQQYVADVQR AIEANAAREF ECLWNEAKRT GKPKSVLSDE LSVAIVDLRK NLESTNLWDN
ESLRRLIMRK ALPAKLLESL DLDTILGRVP VNYLKAIFGA YLASHFVYEY GAVPSQFAFF
EFMSKFYAQA ETSA
//
