ID J3JDR1_9EURY Unreviewed; 430 AA.
AC J3JDR1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=HSB1_40700 {ECO:0000313|EMBL:EJN57709.1};
OS Halogranum salarium B-1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae.
OX NCBI_TaxID=1210908 {ECO:0000313|EMBL:EJN57709.1, ECO:0000313|Proteomes:UP000007813};
RN [1] {ECO:0000313|EMBL:EJN57709.1, ECO:0000313|Proteomes:UP000007813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-1 {ECO:0000313|EMBL:EJN57709.1,
RC ECO:0000313|Proteomes:UP000007813};
RX PubMed=23144405; DOI=10.1128/JB.01815-12;
RA Kim K.K., Lee K.C., Lee J.S.;
RT "Draft Genome Sequence of the Extremely Halophilic Archaeon Halogranum
RT salarium B-1T.";
RL J. Bacteriol. 194:6659-6659(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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJN57709.1}.
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DR EMBL; ALJD01000012; EJN57709.1; -; Genomic_DNA.
DR RefSeq; WP_009377591.1; NZ_ALJD01000012.1.
DR AlphaFoldDB; J3JDR1; -.
DR PATRIC; fig|1210908.3.peg.3834; -.
DR eggNOG; arCOG01352; Archaea.
DR OrthoDB; 6425at2157; -.
DR Proteomes; UP000007813; Unassembled WGS sequence.
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 197..427
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 120
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT SITE 160
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 430 AA; 47128 MW; C4A842003346F6DC CRC64;
MAQTTSESVD ETETNETTES ALTTARRQLK RAATHVDVDS GVVERLKHPT KVQRVSVPLK
RDDGELEVLT GYRAQHDDVR GPYKGGLRYH PEVNADECIG LSMWMTWKCA VMDIPFGGGK
GGIAVDPKSL SDEEKERLTR RFAEELRDVV GPKQDVPAPD MGTDAQTMAW FMDAYSMQRG
ETTPGVVTGK PPVIGGSYGR EEAPGRSVAI ITREAIEYYD WDIEDTTVAV QGYGSVGANA
ARALDEWGAD VVAVSDVDGA IYDPNGLDTK DVMGHEERPG MVSGYDAPET RSNEELLELD
VDVLVPAAVG NVLTADNADD VQANLVVEGA NGPTTFAADT IFEERGIPVV PDILANAGGV
TVSYFEWLQD INRRQWSLDR VHDELESEML QAWNAVRKEV ENRDVTWRDA AYIVALTRVA
TAKETRGLWP
//
