ID Q5YQU8_NOCFA Unreviewed; 458 AA.
AC Q5YQU8;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN OrderedLocusNames=NFA_45920 {ECO:0000313|EMBL:BAD59443.1};
OS Nocardia farcinica (strain IFM 10152).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=247156 {ECO:0000313|EMBL:BAD59443.1, ECO:0000313|Proteomes:UP000006820};
RN [1] {ECO:0000313|EMBL:BAD59443.1, ECO:0000313|Proteomes:UP000006820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 10152 {ECO:0000313|EMBL:BAD59443.1,
RC ECO:0000313|Proteomes:UP000006820};
RX PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA Shiba T., Hattori M.;
RT "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
CC -!- SUBUNIT: Homohexamer. {ECO:0000256|ARBA:ARBA00011643}.
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; AP006618; BAD59443.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5YQU8; -.
DR STRING; 247156.NFA_45920; -.
DR KEGG; nfa:NFA_45920; -.
DR eggNOG; COG0334; Bacteria.
DR HOGENOM; CLU_025763_2_1_11; -.
DR Proteomes; UP000006820; Chromosome.
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; cd05313; NAD_bind_2_Glu_DH; 1.
DR Gene3D; 1.10.285.10; Glutamate Dehydrogenase, chain A, domain 3; 2.
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; IPR014362; Glu_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR033922; NAD_bind_Glu_DH.
DR PANTHER; PTHR43571; NADP-SPECIFIC GLUTAMATE DEHYDROGENASE 1-RELATED; 1.
DR PANTHER; PTHR43571:SF1; NADP-SPECIFIC GLUTAMATE DEHYDROGENASE 1-RELATED; 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.
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:UP000006820}.
FT DOMAIN 215..456
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 138
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 222
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 253
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 390
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 178
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 458 AA; 49924 MW; ECBFC7EB68E84756 CRC64;
MEAGRKIARM AVLDEKLHEV YEEILRRNPG EIEFHQAAFE VLESLGPVVA KHPEYTDGAV
LRRLCEPERQ IIFRVPWVDD QGRVQINRGF RVEFNSALGP YKGGLRFHPS VYLGIVKFLG
FEQIFKNSLT GMPIGGGKGG SDFDPKGRSD GEVMRFCQSF MTELYRHIGE YTDVPAGDIG
VGGREIGYLF GQYKRITNRY ESGVLTGKGL TWGGSQVRPE ATGYGTVFFV DEILRSRGDS
FEGKKVVVSG SGNVAVFAIE KVEQLGGTVV ACSDSGGYVV DDKGIDLDLL KDLKQVRRGR
MCDYVEERGG TARYVENQSV WDVPCDIALP CATQNELDGE AAATLIRNGV RIVAEGANMP
CTPEAARAFT EAGVTFAPGK AVNAGGVATS ALEMQQNASR DSWSFEHTEE RLAEIMRGIH
DRCLETADEY GSPGSYTAGA NIAGFTRVAD AMLALGII
//
