ID A0A0A1DL04_NOCSI Unreviewed; 424 AA.
AC A0A0A1DL04;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN Name=gdhA {ECO:0000313|EMBL:GEB13290.1};
GN ORFNames=KR76_11765 {ECO:0000313|EMBL:AIY17263.1}, NSI01_16050
GN {ECO:0000313|EMBL:GEB13290.1};
OS Nocardioides simplex (Arthrobacter simplex).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Pimelobacter.
OX NCBI_TaxID=2045 {ECO:0000313|EMBL:AIY17263.1, ECO:0000313|Proteomes:UP000030300};
RN [1] {ECO:0000313|EMBL:AIY17263.1, ECO:0000313|Proteomes:UP000030300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-2033D {ECO:0000313|EMBL:AIY17263.1,
RC ECO:0000313|Proteomes:UP000030300};
RX PubMed=25573942;
RA Shtratnikova V.Y., Schelkunov M.I., Pekov Y.A., Fokina V.V.,
RA Logacheva M.D., Sokolov S.L., Bragin E.Y., Ashapkin V.V., Donova M.V.;
RT "Complete Genome Sequence of Steroid-Transforming Nocardioides simplex VKM
RT Ac-2033D.";
RL Genome Announc. 3:0-0(2015).
RN [2] {ECO:0000313|EMBL:GEB13290.1, ECO:0000313|Proteomes:UP000318936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 12069 {ECO:0000313|EMBL:GEB13290.1,
RC ECO:0000313|Proteomes:UP000318936};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Pimelobacter simplex NBRC 12069.";
RL Submitted (JUN-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|PIRNR:PIRNR000185,
CC ECO:0000256|RuleBase:RU004417}.
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DR EMBL; CP009896; AIY17263.1; -; Genomic_DNA.
DR EMBL; BJMC01000008; GEB13290.1; -; Genomic_DNA.
DR RefSeq; WP_038678476.1; NZ_JAAARG010000238.1.
DR AlphaFoldDB; A0A0A1DL04; -.
DR STRING; 2045.KR76_11765; -.
DR KEGG; psim:KR76_11765; -.
DR eggNOG; COG0334; Bacteria.
DR HOGENOM; CLU_025763_1_2_11; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000030300; Chromosome.
DR Proteomes; UP000318936; 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; cd01076; NAD_bind_1_Glu_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; IPR014362; Glu_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR033922; NAD_bind_Glu_DH.
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 PIRSF; PIRSF000185; Glu_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:PIRSR000185-2};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000185-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000185};
KW Reference proteome {ECO:0000313|Proteomes:UP000030300}.
FT DOMAIN 191..421
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 114
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 198
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 357
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 154
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 424 AA; 45156 MW; A35F0B30E84B033D CRC64;
MTALHEPVAA TATGPLADAR EQLREATTLL GYDEGLHQML ATPRREVTVS IPLRRDDGTT
ELFVGHRVQH NFSRGPAKGG LRYSPDVSLD EVRALAMWMT WKCALLDVPY GGAKGGVRID
PRSYSQAELE RVTRRYTSEI SPLIGPERDI PAPDIGTDEK TMAWLMDTYS VQQGHTVLGV
TTGKPISLGG SRGRATATSR GVVHVALAAL RSQGIAPEEA TASVQGFGKV GRYAARFLAE
AGTRVVAVSD QYGAVAAEAG LDIPGLERHV DATGSVVGFA GGDEIAAEAV LEAEVDLLVP
AAVEGVLRGD NAGRVRAKVI VEGANGPTTP EADRILQEAG RLVVPDILAN AGGVIVSYFE
WVQANQAYWW SEIEVEARLA ERMLAAWDSV NAAAARLDVP LRTAATCLAV ERVAQAHQLR
GLYP
//
