ID   C1CXN0_DEIDV            Unreviewed;       343 AA.
AC   C1CXN0;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Putative Glu/Leu/Phe/Val dehydrogenase, Branched-chain amino acid dehydrogenase {ECO:0000313|EMBL:ACO44836.1};
GN   OrderedLocusNames=Deide_00380 {ECO:0000313|EMBL:ACO44836.1};
OS   Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO44836.1, ECO:0000313|Proteomes:UP000002208};
RN   [1] {ECO:0000313|EMBL:ACO44836.1, ECO:0000313|Proteomes:UP000002208}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115
RC   {ECO:0000313|Proteomes:UP000002208};
RX   PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA   de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA   Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA   Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT   "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT   bacterium Deinococcus deserti.";
RL   PLoS Genet. 5:E1000434-E1000434(2009).
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|RuleBase:RU004417}.
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DR   EMBL; CP001114; ACO44836.1; -; Genomic_DNA.
DR   RefSeq; WP_012691959.1; NC_012526.1.
DR   AlphaFoldDB; C1CXN0; -.
DR   STRING; 546414.Deide_00380; -.
DR   PaxDb; 546414-Deide_00380; -.
DR   KEGG; ddr:Deide_00380; -.
DR   eggNOG; COG0334; Bacteria.
DR   HOGENOM; CLU_025763_0_0_0; -.
DR   OrthoDB; 9803297at2; -.
DR   Proteomes; UP000002208; Chromosome.
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; cd01075; NAD_bind_Leu_Phe_Val_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; IPR016211; Glu/Phe/Leu/Val/Trp_DH_bac/arc.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42722; LEUCINE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42722:SF1; VALINE DEHYDROGENASE; 1.
DR   Pfam; PF00208; ELFV_dehydrog; 2.
DR   Pfam; PF02812; ELFV_dehydrog_N; 1.
DR   PIRSF; PIRSF000188; Phe_leu_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.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|PIRSR:PIRSR000188-2};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000188-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU004417};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002208}.
FT   DOMAIN          141..342
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   BINDING         177..182
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ   SEQUENCE   343 AA;  36122 MW;  6D5438786CBCCB69 CRC64;
     MLILEEMQSR GHEALTLLHH APTGLRAALA IHSTVLGPAI AGVRLRDQDE ELAVRGALAL
     SESLTLKAAL AGLNYGGGAC VLMMPEAGVE DPHAREALFR ALGRQVHPMA SRVVLTEDIG
     VTPADIAFLA QETPSTLGMN TDTSSVTGYG VYRGIKAAAR HALGSESMRG VRVAIVGVGA
     VGRSLAMHLH REGARLTISD ERQDRAVALA DELDNVNVAG VGEILDTPCD ILSPCGYGHS
     IRSEDVPRLQ CRLIAGGEHH PLTRKGEGAV KEAGIVYMPD YAINAAGLIA AATGSDATHA
     AERVYQTVNR IVAAAEQYGK APHVVARRMA ERRIDLIGSL GRA
//