ID   A0A1I3AT37_9MICO        Unreviewed;       359 AA.
AC   A0A1I3AT37;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Glu/Leu/Phe/Val dehydrogenase family protein {ECO:0000313|EMBL:TFB88006.1};
GN   ORFNames=E3O11_02715 {ECO:0000313|EMBL:TFB88006.1};
OS   Cryobacterium levicorallinum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Cryobacterium.
OX   NCBI_TaxID=995038 {ECO:0000313|EMBL:TFB88006.1, ECO:0000313|Proteomes:UP000297963};
RN   [1] {ECO:0000313|EMBL:TFB88006.1, ECO:0000313|Proteomes:UP000297963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hh34 {ECO:0000313|EMBL:TFB88006.1,
RC   ECO:0000313|Proteomes:UP000297963};
RA   Liu Q., Xin Y.-H.;
RT   "Genomics of glacier-inhabiting Cryobacterium strains.";
RL   Submitted (MAR-2019) 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   -!- 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:TFB88006.1}.
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DR   EMBL; SOFE01000004; TFB88006.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I3AT37; -.
DR   STRING; 995038.SAMN05216274_10790; -.
DR   Proteomes; UP000297963; 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   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; 1.
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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU004417}.
FT   DOMAIN          156..359
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
SQ   SEQUENCE   359 AA;  36415 MW;  F7FBFBAF1040550E CRC64;
     MTLTHPAAAL DSLAQIPLSH EKVLITTGER SGLLITVAVH STRLGQALGG ARLWQYATWT
     DAVADALRLS AAMTLKNAAA GLNLGGGKSV IYLPLGTVLT DAEKRLAMLD LGDAIESLNG
     AYMTAEDVGT SAELMAIVAE RTNHVCGLPA ASGGVGEPAD ATAAGVYASI ESTLEALFGS
     REVRGRHLVI SGLGQVGGRL ARALAAAGAT LTVTDINPDK HALAEELGAS WVSVADAHRV
     HADLFVPCGL GGVLTSGVIA ELNVLGVCGA ANNQLAVPAG ADQLGARGIL WAPDFVVNAG
     GVVYLAMASE PNADLGQITA RVAAIGTVLT QIFTDARASE ITTLAAAEML AAARLHAAR
//