ID I7CRX3_NATSJ Unreviewed; 436 AA.
AC I7CRX3;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN OrderedLocusNames=NJ7G_1599 {ECO:0000313|EMBL:AFO56843.1};
OS Natrinema sp. (strain J7-2).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=406552 {ECO:0000313|EMBL:AFO56843.1, ECO:0000313|Proteomes:UP000006507};
RN [1] {ECO:0000313|EMBL:AFO56843.1, ECO:0000313|Proteomes:UP000006507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J7-2 {ECO:0000313|EMBL:AFO56843.1,
RC ECO:0000313|Proteomes:UP000006507};
RX PubMed=22911826; DOI=10.1371/journal.pone.0041621;
RA Feng J., Liu B., Zhang Z., Ren Y., Li Y., Gan F., Huang Y., Chen X.,
RA Shen P., Wang L., Tang B., Tang X.F.;
RT "The complete genome sequence of Natrinema sp. J7-2, a haloarchaeon capable
RT of growth on synthetic media without amino acid supplements.";
RL PLoS ONE 7:E41621-E41621(2012).
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; CP003412; AFO56843.1; -; Genomic_DNA.
DR RefSeq; WP_014863763.1; NC_018224.1.
DR AlphaFoldDB; I7CRX3; -.
DR STRING; 406552.NJ7G_1599; -.
DR GeneID; 13352088; -.
DR KEGG; nat:NJ7G_1599; -.
DR PATRIC; fig|406552.5.peg.1423; -.
DR eggNOG; arCOG01352; Archaea.
DR HOGENOM; CLU_025763_1_2_2; -.
DR OrthoDB; 6425at2157; -.
DR Proteomes; UP000006507; Chromosome.
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; 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 NCBIfam; NF041398; GluDhGdhB_Halo; 1.
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.
DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000185}.
FT DOMAIN 196..433
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 119
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT SITE 159
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 436 AA; 47397 MW; 1C3EC1544858717B CRC64;
MASQHRSTTT REATAASETA LETARRQLDR VAAQLDVDDA VIERLSHPRA VHEVTVPLER
DDGSVEVFTG YRAQHDSVRG PYKGGLRYHP DVTRDECVGL SMWMTWKCAV MDLPFGGAKG
GVVVDPKSLS DDETERLTRR FAQEIRDVIG PNTDIPAPDM GTDPQTMAWL MDAYSMQEGE
TIPGVVTGKP PVIGGSYGRE EAPGRSVAIV TRESCDYYDY PLAETTVAVQ GFGSVGANAA
RLLEEWGATI VAVSDVNGGV YDPDGIDVSA IPSHDEEPEA VTRFATELDA GDDVSRLSNS
ELLELDVDVL VPAAVGNVIT ADNADAIAAD IVVEGANGPT TFAADTILEE RGVHVIPDIL
ANAGGVTVSY FEWLQDINRR QWSKERVNEE LEAEMKTAWN ALKDDVERRN VTWRDAAYAV
ALDRIGDSHE TRGLWP
//
