ID A0A066VH35_TILAU Unreviewed; 371 AA.
AC A0A066VH35;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=glutamate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00012907};
DE EC=1.4.1.4 {ECO:0000256|ARBA:ARBA00012907};
GN ORFNames=K437DRAFT_279156 {ECO:0000313|EMBL:KDN40786.1};
OS Tilletiaria anomala (strain ATCC 24038 / CBS 436.72 / UBC 951).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Georgefischeriales; Tilletiariaceae; Tilletiaria.
OX NCBI_TaxID=1037660 {ECO:0000313|EMBL:KDN40786.1, ECO:0000313|Proteomes:UP000027361};
RN [1] {ECO:0000313|EMBL:KDN40786.1, ECO:0000313|Proteomes:UP000027361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UBC 951 {ECO:0000313|EMBL:KDN40786.1,
RC ECO:0000313|Proteomes:UP000027361};
RG DOE Joint Genome Institute;
RA Toome M., Kuo A., Henrissat B., Lipzen A., Tritt A., Yoshinaga Y., Zane M.,
RA Barry K., Grigoriev I.V., Spatafora J.W., Aimea M.C.;
RT "Draft genome sequence of a rare smut relative, Tilletiaria anomala UBC
RT 951.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|RuleBase:RU004417}.
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:KDN40786.1}.
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DR EMBL; JMSN01000087; KDN40786.1; -; Genomic_DNA.
DR RefSeq; XP_013241501.1; XM_013386047.1.
DR AlphaFoldDB; A0A066VH35; -.
DR STRING; 1037660.A0A066VH35; -.
DR GeneID; 25266885; -.
DR HOGENOM; CLU_025763_2_0_1; -.
DR InParanoid; A0A066VH35; -.
DR OMA; MIMGWMM; -.
DR OrthoDB; 45283at2759; -.
DR Proteomes; UP000027361; Unassembled WGS sequence.
DR GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 1.10.285.10; Glutamate Dehydrogenase, chain A, domain 3; 1.
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; IPR036291; NAD(P)-bd_dom_sf.
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 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.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU004417};
KW Reference proteome {ECO:0000313|Proteomes:UP000027361}.
FT DOMAIN 147..369
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
SQ SEQUENCE 371 AA; 41384 MW; 1EA01221BDAB6F3D CRC64;
MSNLPKESEF ELFYEAYSEE CALSITTVLE RVIQFRVVWE NDKGEWQATR SCRVQHNSVL
GVYKGGLRLH ESVLKLLEFE QIFKNALTGL NIGAGKSGSN FSPYGKRDAE RHIDVDIDVP
AGDIGFSARE GGYFFGKRKK RQNEAWAWGV TDYGTWYFVE HMMTHSECDG TPFKGKKVAI
SGSGQVAQFA ALKVIELGDT VLSLGESKGA LISRDKASWQ KEWIEVVVAI KSNRDELSKL
GNKGGKFQWH SSVAQPWKLL KIDDNEVDGS DANEMPARGC RYVGEGDNTP CNLQVINIFE
HSRIDKRRQR CWYGPGKEGN AGGVAVSGLE MTRNSARLQV TRDEVNAKLQ DIMKAVFDVC
AKEGAAHPTV Y
//
