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Database: UniProt
Entry: A8RI49_GIAIN
LinkDB: A8RI49_GIAIN
Original site: A8RI49_GIAIN 
ID   A8RI49_GIAIN            Unreviewed;       335 AA.
AC   A8RI49;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   24-JAN-2024, entry version 50.
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:ABS53090.1};
OS   Giardia intestinalis (Giardia lamblia).
OC   Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX   NCBI_TaxID=5741 {ECO:0000313|EMBL:ABS53090.1};
RN   [1] {ECO:0000313|EMBL:ABS53090.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C28 {ECO:0000313|EMBL:ABS53090.1};
RX   PubMed=17900812; DOI=10.1016/j.vetpar.2007.08.019;
RA   Souza S.L., Gennari S.M., Richtzenhain L.J., Pena H.F., Funada M.R.,
RA   Cortez A., Gregori F., Soares R.M.;
RT   "Molecular identification of Giardia duodenalis isolates from humans, dogs,
RT   cats and cattle from the state of Sao Paulo, Brazil, by sequence analysis
RT   of fragments of glutamate dehydrogenase (gdh) coding gene.";
RL   Vet. Parasitol. 149:258-264(2007).
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; EF507628; ABS53090.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8RI49; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; IPR033524; Glu/Leu/Phe/Val_DH_AS.
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.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU004417}.
FT   DOMAIN          146..335
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:ABS53090.1"
FT   NON_TER         335
FT                   /evidence="ECO:0000313|EMBL:ABS53090.1"
SQ   SEQUENCE   335 AA;  36713 MW;  DAC0299CF9C817D6 CRC64;
     RVIIFRVPWM DDAGRINVNR GFRVQYNSAL GPYKGGLRFH PSVNLSILKF LGFEQILKNS
     LTTLPMGGGK GGSDFDPKGK SDNEVMRFCQ SFMTELQRHV GADTDVPAGD IGVGAREIGY
     LFGQYKRLRN EFTGVLTGKN IKWGGSLIRP EATGYGAVYF LEEMCKDNNT IIRGKNVLLS
     GSGNVAQFAC EKLLQLGAKV LTFSDSNGTI VDKDGFNEEK LTHLKYLKNE KRGRISEFKD
     KYPSVTYYEN KKPWECFEGQ VDCIMPCATQ NEVTGDDATR LVGLGLKFVA EGANMPSTAE
     AVHIYHAKGV MYGPAKAANA GGVSVSGLEM SQNSV
//
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