ID Q23ZD8_TETTS Unreviewed; 500 AA.
AC Q23ZD8;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=TTHERM_00787250 {ECO:0000313|EMBL:EAS01919.1};
OS Tetrahymena thermophila (strain SB210).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=312017 {ECO:0000313|EMBL:EAS01919.1, ECO:0000313|Proteomes:UP000009168};
RN [1] {ECO:0000313|Proteomes:UP000009168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168};
RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA Hamilton E.P., Orias E.;
RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT model eukaryote.";
RL PLoS Biol. 4:1620-1642(2006).
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=1.4.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00023525};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH +
CC NH4(+); Xref=Rhea:RHEA:11612, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.4.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00023549};
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; GG662552; EAS01919.1; -; Genomic_DNA.
DR RefSeq; XP_001022164.1; XM_001022164.3.
DR AlphaFoldDB; Q23ZD8; -.
DR STRING; 312017.Q23ZD8; -.
DR EnsemblProtists; EAS01919; EAS01919; TTHERM_00787250.
DR GeneID; 7831209; -.
DR KEGG; tet:TTHERM_00787250; -.
DR eggNOG; KOG2250; Eukaryota.
DR HOGENOM; CLU_025763_1_0_1; -.
DR InParanoid; Q23ZD8; -.
DR OMA; PCFAAFP; -.
DR OrthoDB; 312189at2759; -.
DR Proteomes; UP000009168; Unassembled WGS sequence.
DR GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR CDD; cd01076; NAD_bind_1_Glu_DH; 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; IPR014362; Glu_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR033922; NAD_bind_Glu_DH.
DR PANTHER; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11606:SF13; GLUTAMATE DEHYDROGENASE 1, MITOCHONDRIAL; 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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000185};
KW Reference proteome {ECO:0000313|Proteomes:UP000009168}.
FT DOMAIN 216..495
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 134
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT SITE 176
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 500 AA; 55628 MW; 311AA4923C9ADC2E CRC64;
MLSKLFKTPV NSLYSSMISR AAFSNISKCK TDESITHMVN YYLDEAAEHT DIPKDKMNFY
KNCDGIVQIN IPLKRENGKF ETIKAYRVQH KTHCLPTKGG FIINDQVSRE DIQSFAVLNT
VRSTTLDLPY GGAKGAICIN PKEYTENELE LIIRRFTLEA AKKNIIGSSV DVLGTDLGAS
EREMNWIKDT FATLYGQDDI HAIACVTGKG LNQGGLKGYV ESPGYGVYYT LKYMLENKEF
LQKTGLTQGL KGKTFVIEGF GSVGYWAAHH LQEAGAILVG VCEHDGQIFN PQGIDASELN
NYMKKNKGVK GFPKATEQEN VAYSKCDFFI PCFFAQSIYA ENADKFQCKV VAEGANLPTT
PAAEKILKEK GIEIIPDIIT SSGGFLASYF EWIKNINHTQ HGAMTRKWEE KSNQQVLETI
EGTTGLRLVS KAILDHVEEI KGASERDLVI SGIEESFENA LIETIETSKK HNVSLRCAAY
INALNKLHGH YEQVGITFSK
//
