ID A0A1H5M0M9_9ACTN Unreviewed; 392 AA.
AC A0A1H5M0M9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=SAMN05216489_08459 {ECO:0000313|EMBL:SEE82088.1};
OS Streptomyces sp. 3213.3.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1855348 {ECO:0000313|EMBL:SEE82088.1, ECO:0000313|Proteomes:UP000198754};
RN [1] {ECO:0000313|EMBL:SEE82088.1, ECO:0000313|Proteomes:UP000198754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3213 {ECO:0000313|EMBL:SEE82088.1,
RC ECO:0000313|Proteomes:UP000198754};
RA de Groot N.N.;
RL Submitted (OCT-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; FNTK01000001; SEE82088.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5M0M9; -.
DR STRING; 1855348.SAMN05216489_08459; -.
DR Proteomes; UP000198754; Unassembled WGS sequence.
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 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 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:UP000198754}.
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 392 AA; 41585 MW; D4E0204B78C2C79C CRC64;
MTAPLMSLTW TDHVTGRQGF LVVDRLVRGV SSGGLRMRPG CTLDEVAGLA RGMTMKEALH
YDPAGRYIPL GGAKGGIDCD PQDPESYGLL VRYLRAMRPY VESFWTTGED LGLSQDLVDR
AAAEAGLVSS IQAVYPLLDD EAAARRRLAD AFAVEVDGIG LDELVGGCGV AESVLAALDR
AGVPYAGTRV AVQGLGTMGG ATARFLTRAG LTIVAVADVK GTIVNPAGLD VDALLAARDA
YGTVDRSVLR PGDRELPGGD WLSVEAEVLV PAAVSYAVDT TNQGAVTARW IVEAANMPVL
PEAEERLSAR GVVVLPDVVV NSGTNAWWWW TLFGDIGADA DEAFAHTRRS MRALIELMLA
RAEADGTTPR AAAHAIVADR LPVIAERFGW YR
//
