ID D8J3W2_HALJB Unreviewed; 423 AA.
AC D8J3W2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN OrderedLocusNames=HacjB3_00300 {ECO:0000313|EMBL:ADJ13453.1};
GN ORFNames=C497_19032 {ECO:0000313|EMBL:ELY33072.1};
OS Halalkalicoccus jeotgali (strain DSM 18796 / CECT 7217 / JCM 14584 / KCTC
OS 4019 / B3).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halococcaceae; Halalkalicoccus.
OX NCBI_TaxID=795797 {ECO:0000313|EMBL:ADJ13453.1, ECO:0000313|Proteomes:UP000000390};
RN [1] {ECO:0000313|EMBL:ADJ13453.1, ECO:0000313|Proteomes:UP000000390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B3 {ECO:0000313|EMBL:ADJ13453.1}, and DSM 18796 / CECT 7217 /
RC JCM 14584 / KCTC 4019 / B3 {ECO:0000313|Proteomes:UP000000390};
RX PubMed=20601480; DOI=10.1128/JB.00663-10;
RA Roh S.W., Nam Y.D., Nam S.H., Choi S.H., Park H.S., Bae J.W.;
RT "Complete genome sequence of Halalkalicoccus jeotgali B3(T), an extremely
RT halophilic archaeon.";
RL J. Bacteriol. 192:4528-4529(2010).
RN [2] {ECO:0000313|Proteomes:UP000011645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B3 {ECO:0000313|Proteomes:UP000011645};
RA Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., Darling A.,
RA Eisen J.A., Facciotti M.T.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ELY33072.1, ECO:0000313|Proteomes:UP000011645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B3 {ECO:0000313|EMBL:ELY33072.1,
RC ECO:0000313|Proteomes:UP000011645};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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; CP002062; ADJ13453.1; -; Genomic_DNA.
DR EMBL; AOHV01000045; ELY33072.1; -; Genomic_DNA.
DR RefSeq; WP_008419122.1; NZ_AXZD01000013.1.
DR AlphaFoldDB; D8J3W2; -.
DR STRING; 795797.HacjB3_00300; -.
DR GeneID; 9417853; -.
DR KEGG; hje:HacjB3_00300; -.
DR PATRIC; fig|795797.18.peg.61; -.
DR eggNOG; arCOG01352; Archaea.
DR HOGENOM; CLU_025763_1_2_2; -.
DR OrthoDB; 6425at2157; -.
DR Proteomes; UP000000390; Chromosome.
DR Proteomes; UP000011645; 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 191..420
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 114
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT SITE 154
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 423 AA; 45564 MW; E7757DBE26D472F9 CRC64;
MSVPVTEERA EPETALATAR RQLDRAAAHV EIDPAVVERL KHPARVQRVS LPVERDDGSL
EVFTGYRAQH DSVRGPFKGG MRYHPGVTEE ECIGLSMWMT WKTAVMDLPF GGAKGGVVVD
PKELSEAETE RLTRRFAQEL RDTVGPMHDI PAPDMGTDAE TMGWFMDAYS VLQGETTPGV
VTGKPPVIGG SHGREEAPGR SVAIVAREAC DYHDIPIEGA TVAVQGYGSV GANAARLLDS
WGATVVAVSD VNGAAYDPDG LDTASIPSHE EEPEAVTRVA ERTIENEELL ELDVDVLVPA
AVGNVITAAN ADAIAANLVV EGANGPTTAT ADSILRERGI PVIPDILANA GGVTVSYFEW
LQDINRRSWS HERVNEELET EMLRAWSAVA DRVDERGLAW RDAAYVLALE RLGAAHDARG
LWP
//
