ID A0A0W1RDQ6_9EURY Unreviewed; 433 AA.
AC A0A0W1RDQ6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=AUR64_03365 {ECO:0000313|EMBL:KTG11553.1};
OS Haloprofundus marisrubri.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloprofundus.
OX NCBI_TaxID=1514971 {ECO:0000313|EMBL:KTG11553.1, ECO:0000313|Proteomes:UP000054387};
RN [1] {ECO:0000313|EMBL:KTG11553.1, ECO:0000313|Proteomes:UP000054387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB9 {ECO:0000313|EMBL:KTG11553.1,
RC ECO:0000313|Proteomes:UP000054387};
RA Zhang G., Stingl U., Rashid M.;
RT "Haloprofundus marisrubri gen. nov., sp. nov., an extremely halophilic
RT archaeon isolated from the Discovery deep brine-seawater interface in the
RT Red Sea.";
RL Submitted (DEC-2015) 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}.
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:KTG11553.1}.
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DR EMBL; LOPU01000003; KTG11553.1; -; Genomic_DNA.
DR RefSeq; WP_058580037.1; NZ_LOPU01000003.1.
DR AlphaFoldDB; A0A0W1RDQ6; -.
DR STRING; 1514971.AUR64_03365; -.
DR OrthoDB; 6425at2157; -.
DR Proteomes; UP000054387; 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 201..430
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 124
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT SITE 164
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 433 AA; 47415 MW; DF4A717BDDBF5CB2 CRC64;
MVSTSESRHD SVTDTRADPV ESESALETAR RQLHHAADRL EIDPNVVERL KHPQKVHEVT
IPIERDDGTV EVFTGYRAQH DSVRGPFKGG LRYHPDVTRD ECVGLGMWMT WKCAVMDLPF
GGAKGGVAVN PKELSAEENE RLTRRFAQEL RDVIGPNQDI PAPDMGTDSQ TMAWLMDAYS
MQKGETTPGV VTGKPPVVGG SQGRQEAPGR SVAIVTKLLC EYYDRPLEET TVAVQGYGSV
GASAARLLDD WGATVVAVSD VNGAMYDPSG IDTATVPSHD DEPEAVTTYA DEVISNDELL
TLDVDVLVPA ALGNVITRRN AENIAAEFVV EGANGPTTSA ADSILEERGI EVIPDILANA
GGVTVSYFEW LQDINRRAWS LERVNNELET EMCSAWRAVK TEYERRDVTW RDAAYIVALS
RIAEAHEVRG LWP
//
