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Database: UniProt
Entry: A0A1G7WZE5_9PSEU
LinkDB: A0A1G7WZE5_9PSEU
Original site: A0A1G7WZE5_9PSEU 
ID   A0A1G7WZE5_9PSEU        Unreviewed;       313 AA.
AC   A0A1G7WZE5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Leucine dehydrogenase {ECO:0000313|EMBL:SDG77297.1};
GN   ORFNames=SAMN05216553_111164 {ECO:0000313|EMBL:SDG77297.1};
OS   Lentzea fradiae.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Lentzea.
OX   NCBI_TaxID=200378 {ECO:0000313|EMBL:SDG77297.1, ECO:0000313|Proteomes:UP000199623};
RN   [1] {ECO:0000313|Proteomes:UP000199623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3506 {ECO:0000313|Proteomes:UP000199623};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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}.
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DR   EMBL; FNCC01000011; SDG77297.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7WZE5; -.
DR   STRING; 200378.SAMN05216553_111164; -.
DR   OrthoDB; 9803297at2; -.
DR   Proteomes; UP000199623; Unassembled WGS sequence.
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   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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000188-2};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000188-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU004417}.
FT   DOMAIN          136..306
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        72
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT   BINDING         174..179
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ   SEQUENCE   313 AA;  32778 MW;  E730E6D38FEBB771 CRC64;
     MWEHERLVVR TGKRSGMTTM VAVHSTAAGP AVGGCRMKAY GQITDAVADV LRLSKAMTLK
     CAAAGVPHGG AKSVIVVDRP LTPELRRDVL LDHAELVDEF GGTYRAAPDV GTGPEDMVVL
     NEITPFVYCL PEERGGTGSS SGPTARGVLA ALRAASNHVF GTEDLAGKKV VVSGFGAVGR
     LVAEGLTAAD VTVSDVDENR RTDRYGWVHP DEAYRVEADV LVPAAVGGVL SPETAAGLKV
     KLVVGPANNQ LTDDGVADLL AERGIVWVPD HIASAGGVIY TLAREDDGVD HETALKRVDA
     IETTVRELLG TGR
//
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