ID A0A1M5UV70_9ACTN Unreviewed; 407 AA.
AC A0A1M5UV70;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=SAMN05444521_1348 {ECO:0000313|EMBL:SHH66875.1};
OS Streptomyces sp. 3214.6.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1882757 {ECO:0000313|EMBL:SHH66875.1, ECO:0000313|Proteomes:UP000190947};
RN [1] {ECO:0000313|Proteomes:UP000190947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3124.6 {ECO:0000313|Proteomes:UP000190947};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|PIRNR:PIRNR000185}.
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DR EMBL; LT670819; SHH66875.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M5UV70; -.
DR STRING; 1882757.SAMN05444521_1348; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000190947; Chromosome i.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProt.
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; 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 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000185};
KW Reference proteome {ECO:0000313|Proteomes:UP000190947}.
FT DOMAIN 158..389
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 74
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
SQ SEQUENCE 407 AA; 43001 MW; 862650F3CBF7D6F4 CRC64;
MTTPFLSLTW TDHVTGRQGF LVVDRLVRGV CSGGLRMRPG CSLQEVAGLA HGMSLKEALH
YDPEARYVPL GGAKGGIDCD PRDPQAYGLL VRYLRAVRPY VESCWTTGED LGLTQDLVDR
AAAEAGLVSS VQAVYPLLDD EAAARARLAA AFAVEVDGIG LDELVGGLGV AESVLTALDR
AGEAYAGTRV ALQGLGTMGG ATARFLTRAG LTVVAVADIK GTIANPAGLD VEALLAARDA
HGAVDRAVLR PGDRELPGDA WLSVDAEVLV PAAVSYAIGV EEQEFIGARW IAEAANMPVL
PEAEKLLHAR GVIVLPDVVV NSGTNAWWWW TLFGDIGADA EEAFAYTRRS MRALVELVLA
RAETDGTTPR AAAHTIAARR LPVIAERFGH HRPAPNAHAP ARCAPTD
//
