ID A0A0Q8PYH9_9ACTN Unreviewed; 412 AA.
AC A0A0Q8PYH9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Amino acid dehydrogenase {ECO:0000313|EMBL:KRB78438.1};
GN ORFNames=ASE01_04000 {ECO:0000313|EMBL:KRB78438.1};
OS Nocardioides sp. Root190.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736488 {ECO:0000313|EMBL:KRB78438.1, ECO:0000313|Proteomes:UP000050886};
RN [1] {ECO:0000313|EMBL:KRB78438.1, ECO:0000313|Proteomes:UP000050886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root190 {ECO:0000313|EMBL:KRB78438.1,
RC ECO:0000313|Proteomes:UP000050886};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB78438.1, ECO:0000313|Proteomes:UP000050886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root190 {ECO:0000313|EMBL:KRB78438.1,
RC ECO:0000313|Proteomes:UP000050886};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382}.
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:KRB78438.1}.
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DR EMBL; LMIA01000007; KRB78438.1; -; Genomic_DNA.
DR RefSeq; WP_056749059.1; NZ_LMIA01000007.1.
DR AlphaFoldDB; A0A0Q8PYH9; -.
DR STRING; 1736488.ASE01_04000; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000050886; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; 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 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 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 Reference proteome {ECO:0000313|Proteomes:UP000050886}.
FT DOMAIN 181..412
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
SQ SEQUENCE 412 AA; 44434 MW; 65EA9B62C016E0A6 CRC64;
MKNLLDRFEA TAPEIVFEWH DAETEAKGWA VINSLRGGAA GGGTRMRAGL DRSEVEALAK
TMEVKFTVSG PAIGGAKSGI DFDPNDPRRE GVLARWFKAV SPLLKTYYGT GGDLNVDEVH
DVIPLTERYG LWHPQQGIVN GHFAADEREL VQRVGMLRLG VSKVVEDPRY TPDREAKYTI
ADMVTGWGVA ESVVHYYATY GAAQGQSLAG KRVIVQGWGN VGSAAAFYLA QAGARVVGII
DRDGGLMNPD GFTPEEVRAL FVGKQGNALR AESLIGFAEL DDTIWDMGAE IFLPCAASRL
VTVEHVKRLV SAGLELISAG ANVPFADPEI FYGPTYEFAD QHVAVIPDFI ANCGMARTFT
LLMEGIGEVS DEMILGDVSR TIRTALAACH ERSPHPTLVA ATALEIALDQ LV
//
