ID G9I719_GIAIN Unreviewed; 169 AA.
AC G9I719;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 29.
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:AEV23621.1};
OS Giardia intestinalis (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=5741 {ECO:0000313|EMBL:AEV23621.1};
RN [1] {ECO:0000313|EMBL:AEV23621.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ISSGdA387 {ECO:0000313|EMBL:AEV23621.1}, and ISSGDA387_b
RC {ECO:0000313|EMBL:AEV23622.1};
RX PubMed=22022810; DOI=10.1089/vbz.2011.0751;
RA Beck R., Sprong H., Pozio E., Caccio S.M.;
RT "Genotyping Giardia duodenalis Isolates from Dogs: Lessons from a
RT Multilocus Sequence Typing Study.";
RL Vector Borne Zoonotic Dis. 12:206-213(2012).
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; JN587359; AEV23621.1; -; Genomic_DNA.
DR EMBL; JN587360; AEV23622.1; -; Genomic_DNA.
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; 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 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|RuleBase:RU004417}.
FT DOMAIN 50..168
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:AEV23621.1"
FT NON_TER 169
FT /evidence="ECO:0000313|EMBL:AEV23621.1"
SQ SEQUENCE 169 AA; 18940 MW; 79166F203CDE4279 CRC64;
QRHVGADTDV PAGDIGVGAR EIGYLFGQYK RLRNEFTGVL TGKNIKWGGS LIRPEATGYG
AVYFLEEMCK DNNTIIRGKN VLLSGSGNVA QFACEKLLQL GAKVLTFSDS NGTIVDKDGF
NEEKLTHLKY LKNEKRGRIS EFKDKYPSVX YYENKKPWEC FEGQVDCIM
//