ID A0A1B1E765_9APIC Unreviewed; 511 AA.
AC A0A1B1E765;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=PCOAH_00048350 {ECO:0000313|EMBL:ANQ10599.1};
OS Plasmodium coatneyi.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium.
OX NCBI_TaxID=208452 {ECO:0000313|EMBL:ANQ10599.1, ECO:0000313|Proteomes:UP000092716};
RN [1] {ECO:0000313|Proteomes:UP000092716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hackeri {ECO:0000313|Proteomes:UP000092716};
RA Chien J.-T., Pakala S.B., Geraldo J.A., Lapp S.A., Barnwell J.W.,
RA Kissinger J.C., Galinski M.R., Humphrey J.C.;
RT "First high quality genome sequence of Plasmodium coatneyi using continuous
RT long reads from single molecule, real-time sequencing.";
RL Submitted (JUN-2016) 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; CP016251; ANQ10599.1; -; Genomic_DNA.
DR RefSeq; XP_019917294.1; XM_020061618.1.
DR AlphaFoldDB; A0A1B1E765; -.
DR EnsemblProtists; ANQ10599; ANQ10599; PCOAH_00048350.
DR GeneID; 30911566; -.
DR VEuPathDB; PlasmoDB:PCOAH_00048350; -.
DR OrthoDB; 45283at2759; -.
DR Proteomes; UP000092716; Chromosome 13.
DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProt.
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 Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000185-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000185}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..511
FT /note="Glutamate dehydrogenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008521654"
FT DOMAIN 266..509
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 190
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 273
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 304
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 443
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 230
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 511 AA; 55831 MW; 4DBCCF46F0122C64 CRC64;
MVLSLSAVGL FALISGALGL SKTNHLRHVA PGFLTTEVAK GAHAQGRGRA KLRSNMHSYG
YNGSGSVEDK MDLLRERVKE RNKGEPEFLQ AFEEVLLSLK PLFKKNSAYL GVLENIAEPE
RVIQFRVPWV DDKGEHRMNR GFRVQYSSVL GPYKGGLRFH PTVNLSIIKF LGFEQIFKNS
LTTLPMGGGK GGSDFDPKGK SPNEVLSFCK SFMTNLYRHI GPNTDVPAGD IGVGGREIGY
LFGQYKKLSN AFEGVLTGKN IKWGGSNIRA EATGYGAVYF AENALAKVND SLAGKRCVVS
GSGNVAQYLV EKLLQKGATV LTMSDSDGYI YEPNGFTKEQ LAYVMELKNV KRGRLKEYAD
WSTTCKYVEK GKPWEIPCDL AFPCATQNEI DKKDADLLIK NKCKMVVEGA NMPTHIDAMH
LLKKSGVVIC PSKAANAGGV AVSGLEMSQN SMRLQWTGEE TDQKLQAIMK SIYEQCDGAS
RLYLGESDLV AGANIAGFLK VADSFQEQGG L
//
