ID B5L566_GIAIN Unreviewed; 275 AA.
AC B5L566;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=glutamate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00012907};
DE EC=1.4.1.4 {ECO:0000256|ARBA:ARBA00012907};
DE Flags: Fragment;
GN Name=gdh {ECO:0000313|EMBL:ACB45941.1};
OS Giardia intestinalis (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=5741 {ECO:0000313|EMBL:ACB45941.1};
RN [1] {ECO:0000313|EMBL:ACB45941.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Dolphin 13 {ECO:0000313|EMBL:ACB45943.1}, Gull 1
RC {ECO:0000313|EMBL:ACB45941.1}, Gull 12 {ECO:0000313|EMBL:ACB45947.1},
RC and Seal 10A {ECO:0000313|EMBL:ACB45948.1};
RA Lasek-Nesselquist E., Bogomolni A.L., Gast R.J., Welch D.M., Ellis J.C.,
RA Sogin M.L., Moore M.J.;
RT "Molecular characterization of Giardia intestinalis haplotypes in marine
RT animals: variation and zoonotic potential.";
RL Dis. Aquat. Organ. 81:39-51(2008).
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|RuleBase:RU004417}.
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DR EMBL; EU362965; ACB45941.1; -; Genomic_DNA.
DR EMBL; EU362967; ACB45943.1; -; Genomic_DNA.
DR EMBL; EU362971; ACB45947.1; -; Genomic_DNA.
DR EMBL; EU362972; ACB45948.1; -; Genomic_DNA.
DR AlphaFoldDB; B5L566; -.
DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProt.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU004417}.
FT DOMAIN 76..275
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACB45941.1"
FT NON_TER 275
FT /evidence="ECO:0000313|EMBL:ACB45941.1"
SQ SEQUENCE 275 AA; 29978 MW; 098F09B385E2AC9E CRC64;
GGSDFDPKGK SDNEVMRFCQ SFMTELQRHV GADTDVPAGD IGVGAREIGY LYGQYKRLRN
EFTGVLTGKN VKWGGSFIRP EATGYGAVYF LEEMCKDNNT VIRGKNVLLS GSGNVAQFAC
EKLIQLGAKV LTFSDSNGTI VDKDGFNEEK LAHLMYLKNE KRGRVSEFKD KYPSVAYYEG
KKPWECFEGQ VDCIMPCATQ NEVSGDDATR LVGLGLKFVA EGANMPSTAE AVHVYHAKGV
MYGPAKASNA GGVSVSGLEM SQNSVRLQWT AEEVD
//
