GenomeNet

Database: UniProt
Entry: A0A1M7TCZ0_FERGO
LinkDB: A0A1M7TCZ0_FERGO
Original site: A0A1M7TCZ0_FERGO 
ID   A0A1M7TCZ0_FERGO        Unreviewed;       286 AA.
AC   A0A1M7TCZ0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Glu/Leu/Phe/Val dehydrogenase, dimerisation domain {ECO:0000313|EMBL:SHN68644.1};
GN   ORFNames=SAMN02745226_01858 {ECO:0000313|EMBL:SHN68644.1};
OS   Fervidobacterium gondwanense DSM 13020.
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC   Fervidobacterium.
OX   NCBI_TaxID=1121883 {ECO:0000313|EMBL:SHN68644.1, ECO:0000313|Proteomes:UP000184207};
RN   [1] {ECO:0000313|EMBL:SHN68644.1, ECO:0000313|Proteomes:UP000184207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13020 {ECO:0000313|EMBL:SHN68644.1,
RC   ECO:0000313|Proteomes:UP000184207};
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|RuleBase:RU004417}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FRDJ01000014; SHN68644.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M7TCZ0; -.
DR   STRING; 1121883.SAMN02745226_01858; -.
DR   Proteomes; UP000184207; 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; 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   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.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU004417}.
FT   DOMAIN          50..282
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
SQ   SEQUENCE   286 AA;  30941 MW;  9AD82CEA819F9D22 CRC64;
     MMVGPQKDIP APDVNTNAKI MAWYMDTYSM NVGYTALGVV TGKPLDLGGS EGRPEATGRG
     VAITANEACK ALGKDISKAT VAIQGFGNVG SYSAKILSEE FGAKIVAVSD VSGGIYNENG
     LDVNDVIAYR DANKGIIKGY PKAKPITNEE LLELDVDILV PAALENAITE KNADRIRAKI
     IVEGANGPTT PEAEEVLIKK GVLIVPDILA NAGGVTVSYF EWVQDLQTFF WDIDDIRKKL
     TKMMVNSFAE VYKTKEKYNT DMRTAAYIVA ISRVANAVKE RGYYPM
//
DBGET integrated database retrieval system