ID A0A372IHK6_9RHOB Unreviewed; 349 AA.
AC A0A372IHK6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Glu/Leu/Phe/Val dehydrogenase {ECO:0000313|EMBL:RFU14388.1};
GN ORFNames=DZD18_01995 {ECO:0000313|EMBL:RFU14388.1};
OS Rhodobacteraceae bacterium W635.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=2303578 {ECO:0000313|EMBL:RFU14388.1, ECO:0000313|Proteomes:UP000264655};
RN [1] {ECO:0000313|EMBL:RFU14388.1, ECO:0000313|Proteomes:UP000264655}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W635 {ECO:0000313|EMBL:RFU14388.1,
RC ECO:0000313|Proteomes:UP000264655};
RA Hou X.J.;
RT "Ayaqqumibacter halotolerans gen. nov., sp. nov., isolated from a saline
RT lake in Xinjiang province, China.";
RL Submitted (AUG-2018) 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:RFU14388.1}.
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DR EMBL; QVQC01000008; RFU14388.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372IHK6; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000264655; 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 Coiled coil {ECO:0000256|SAM:Coils}; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000264655}.
FT DOMAIN 143..347
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT COILED 297..324
FT /evidence="ECO:0000256|SAM:Coils"
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 349 AA; 35930 MW; BEF1579AC7551A73 CRC64;
MQIRQIPTES HEEVLRVADD ATGLLAYIAI HSTQLGPAAG GLRMKPYDSE EEALNDALRL
SHGMTFKTAA AGLPLGGGKA VIVGDPAQDK TEALLMAFGR AVAALKGRYW TAEDMGMGPA
DMAVIARETE FVAGRAEGPH ASGDPSPVTA RGIFNAIRCT ARHRFGAADL AGRGVALQGL
GHVGWQLAGL LHEAGARLTV ADMAPARCEA AAGAYGAKVV LAEDILSTEA DILAPCAIGG
VLNGGTVPGL RVKAVAGGAN NQLATPADGD ALQARGILYA PDYVVNAGGI INVATEILRI
EDRARFVTEK LAEAEATLDA ILARAAAQGL APHRIADETV LARMDRAAA
//
