ID B3T4F8_9ARCH Unreviewed; 391 AA.
AC B3T4F8;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=ALOHA_HF4000ANIW133O4ctg2g46 {ECO:0000313|EMBL:ABZ07467.1};
OS uncultured marine crenarchaeote HF4000_ANIW133O4.
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC environmental samples.
OX NCBI_TaxID=455574 {ECO:0000313|EMBL:ABZ07467.1};
RN [1] {ECO:0000313|EMBL:ABZ07467.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18580971; DOI=10.1038/ismej.2008.62;
RA Konstantinidis K.T., Delong E.F.;
RT "Genomic patterns of recombination, clonal divergence and environment in
RT marine microbial populations.";
RL ISME J. 2:1052-1065(2008).
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; EU016600; ABZ07467.1; -; Genomic_DNA.
DR AlphaFoldDB; B3T4F8; -.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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 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 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}.
FT DOMAIN 158..388
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 78
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 37
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 165
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 196
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 324
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 120
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 391 AA; 42867 MW; 951FEFFAD2AF12BE CRC64;
MPNRFLRVKV PVKMDDGKIR VFTGFRCQHN NDRGPYKGGI RYFDPEGGVK YMEREVMALS
SWMTWKCAVV DIPLGGAKGG VFVNPKKEKI SDGELERLTR QFASRIAEVI GPQKDIPAPD
VYTTGKEMTQ IMDTFTKMNG NNYSPGTITG KPIPMGGSLA RDVATGLGNA YCIREAAKIL
NIELKGTKVV LQGFGNASTF SGVYLEKMGA KCIAASDSKG SILVPDGFKV QELIDWKQKE
GSVVGYPGSK EISTEELLTT ECDVLVPGAL ENQITAAIAE KLQCKIIGEA ANGPTLPEAD
PILHKKGVFV IPDILANSGG VCISYLEWVQ NNMGYYWTFD EVASKMEVKI VKGLKDMYEL
SKKHNIDNRK AAMVLAVSRV LEAFNHKGIW P
//
