ID A0A061AZ10_CYBFA Unreviewed; 460 AA.
AC A0A061AZ10;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=BON22_2166 {ECO:0000313|EMBL:ONH68004.1}, CYFA0S_05e02432g
GN {ECO:0000313|EMBL:CDR40614.1};
OS Cyberlindnera fabianii (Yeast) (Hansenula fabianii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX NCBI_TaxID=36022 {ECO:0000313|EMBL:CDR40614.1};
RN [1] {ECO:0000313|EMBL:CDR40614.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YJS4271 {ECO:0000313|EMBL:CDR40614.1};
RX PubMed=25103752; DOI=10.1128/genomeA.00638-14;
RA Freel K.C., Sarilar V., Neuveglise C., Devillers H., Friedrich A.,
RA Schacherer J.;
RT "Genome sequence of the yeast Cyberlindnera fabianii (Hansenula
RT fabianii).";
RL Genome Announc. 2:E00638-E00638(2014).
RN [2] {ECO:0000313|Proteomes:UP000189513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=65 {ECO:0000313|Proteomes:UP000189513};
RX PubMed=28385833; DOI=10.1128/genomeA.00064-17;
RA van Rijswijck I.M.H., Derks M.F.L., Abee T., de Ridder D., Smid E.J.;
RT "Genome sequences of Cyberlindnera fabianii 65, Pichia kudriavzevii 129,
RT and Saccharomyces cerevisiae 131 isolated from fermented masau fruits in
RT Zimbabwe.";
RL Genome Announc. 5:E00064-E00064(2017).
RN [3] {ECO:0000313|EMBL:ONH68004.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=65 {ECO:0000313|EMBL:ONH68004.1};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homohexamer. {ECO:0000256|ARBA:ARBA00011643}.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|PIRNR:PIRNR000185,
CC ECO:0000256|RuleBase:RU004417}.
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DR EMBL; LK052890; CDR40614.1; -; Genomic_DNA.
DR EMBL; MPUK01000003; ONH68004.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061AZ10; -.
DR STRING; 36022.A0A061AZ10; -.
DR VEuPathDB; FungiDB:BON22_2166; -.
DR OMA; MIMGWMM; -.
DR OrthoDB; 45283at2759; -.
DR Proteomes; UP000189513; Unassembled WGS sequence.
DR GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR CDD; cd05313; NAD_bind_2_Glu_DH; 1.
DR Gene3D; 1.10.285.10; Glutamate Dehydrogenase, chain A, domain 3; 2.
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; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR InterPro; IPR014362; Glu_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR033922; NAD_bind_Glu_DH.
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 PIRSF; PIRSF000185; Glu_DH; 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.
DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRSR:PIRSR000185-2};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000185-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000185};
KW Reference proteome {ECO:0000313|Proteomes:UP000189513}.
FT DOMAIN 189..457
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 113
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 196
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 230
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 385
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 153
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 460 AA; 50027 MW; CC16365A46D29A22 CRC64;
MVQPSEPEFE QALNEVYSTL KASSLFEKEP KYEKVLPVIQ IPERIIQFRV VWENDKGELE
VNRGYRVQFN SALGPYKGGL RFHPTVNLSI LKFLGFEQIF KNALTGLAIG GGKGGSDFNP
KGRSNNEIRK FCVAFMRELS RHIGQDTDVP AGDINVGGRE IGYLFGAYKA IRNSWEGVLT
GKGLTWGGSL IRPEATGYGL VYYTEEMIKY ATQNKENFKG KRVAISGSGN VAQYAALKVI
ELGGTVVSLS DSKGSIISES GITKEQIYDI QAAKLKFKSL SEIIGEASSF SKDSVKYVDG
ARPWTQVGQV DVALPCATQN EVSGDEAKAL VAAGCKYVAE GSNMGSTQDA IDVFEGERVA
TASASTPAVW YGPGKASNAG GVLVSALEMA QNSQRMQWTS EKVDEELHTR MIELFKQSIK
YATTYSKESN KEALPSLVMG ANLAGFVKVA DAMFDHGDVF
//
