ID A0A1Q4UNH5_9PROT Unreviewed; 349 AA.
AC A0A1Q4UNH5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Amino acid dehydrogenase {ECO:0000313|EMBL:OKH87015.1};
GN ORFNames=LF95_18635 {ECO:0000313|EMBL:OKH87015.1};
OS Thalassospira sp. TSL5-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Thalassospiraceae; Thalassospira.
OX NCBI_TaxID=1544451 {ECO:0000313|EMBL:OKH87015.1, ECO:0000313|Proteomes:UP000186302};
RN [1] {ECO:0000313|EMBL:OKH87015.1, ECO:0000313|Proteomes:UP000186302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSL5-1 {ECO:0000313|EMBL:OKH87015.1,
RC ECO:0000313|Proteomes:UP000186302};
RA Zhou H., Wang H.;
RT "Genome sequencing of Thalassospira sp. TSL5-1.";
RL Submitted (SEP-2014) 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:OKH87015.1}.
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DR EMBL; JRJD01000005; OKH87015.1; -; Genomic_DNA.
DR RefSeq; WP_073956480.1; NZ_KV880639.1.
DR AlphaFoldDB; A0A1Q4UNH5; -.
DR STRING; 1544451.LF95_18635; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000186302; Unassembled WGS sequence.
DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProt.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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; IPR033524; Glu/Leu/Phe/Val_DH_AS.
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; PS00074; GLFV_DEHYDROGENASE; 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}.
FT DOMAIN 146..348
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 80
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT BINDING 182..187
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 349 AA; 37398 MW; 28FD2F2215037B0F CRC64;
MSIFSDPAFD NHEQVVFASD RETGLKAIIA VHNTHLGPSL GGCRMWPYAS EQDAIHDVLR
LSRGMTYKSA LVNLPLGGGK SVIIGDPRTQ KTPELFRAVG RAVERLNGRY IVAEDVGTSP
ADMAEIARQT HHVGGINDGK DPARTGDPSP FTAYGVFIGL KEAVKHKTGN DDLKDMRVAV
QGLGNVGFHL CELLHNAGAE LIVADINASA VDRAVDRFGA KAVSVDEILS VNADVLAPCA
LGGIINDTSI ASLKAGIIAG AANNQLEADR HGDILREMGV LYAPDYVINA GGVVEVHYCR
EGRPVSETNR HIEGIGATVR EIFERADREN KSTSFIADRL AEERFGKKA
//
