ID A0A0R0CQA4_9GAMM Unreviewed; 365 AA.
AC A0A0R0CQA4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Leucine dehydrogenase {ECO:0000313|EMBL:KRG72188.1};
GN ORFNames=ABB27_02000 {ECO:0000313|EMBL:KRG72188.1};
OS Stenotrophomonas terrae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=405446 {ECO:0000313|EMBL:KRG72188.1, ECO:0000313|Proteomes:UP000051863};
RN [1] {ECO:0000313|EMBL:KRG72188.1, ECO:0000313|Proteomes:UP000051863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18941 {ECO:0000313|EMBL:KRG72188.1,
RC ECO:0000313|Proteomes:UP000051863};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible oxidative deamination of glutamate
CC to alpha-ketoglutarate and ammonia. {ECO:0000256|ARBA:ARBA00003868}.
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:KRG72188.1}.
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DR EMBL; LDJJ01000006; KRG72188.1; -; Genomic_DNA.
DR RefSeq; WP_057626555.1; NZ_LDJJ01000006.1.
DR AlphaFoldDB; A0A0R0CQA4; -.
DR PATRIC; fig|405446.3.peg.3031; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000051863; 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; 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.
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 143..350
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 79
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT BINDING 179..184
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 365 AA; 39685 MW; 42556D4632AC66D4 CRC64;
MLFETLETSG HEQVLFCQNR DAGLKAIIAI HNTTLGPALG GVRMRPYANT DDALRDVLRL
SRTMTYKNAL AGLNVGGGKA VIIGDPRTAK SEVLFRAFGR QVEALAGRYI TAEDVGTDVN
DMENIYLETG FVTGVHQVHG GSGDPAPFTA YGALQALMAS VKRKFGHEEI GKLSIAVQGL
GHIGMELVKL LRERGAKLYV TDLDPVLVQK AVAEYGCEAV KPDAIYDVAA DVFAPCAMEG
AIDMATLERL KAKVICGTAN NQLASHAVGD ELYKRGVLWA PDYAVNAGGV MNVSLEIDGY
NRERAMRLIR SIYHNLGKIF DQSERDEISP QRAADRIAEN RLEAIGKLKM PMGRAVPRMN
RLRGE
//
