ID A0A1B8SLY6_9MYCO Unreviewed; 449 AA.
AC A0A1B8SLY6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN Name=gdhA {ECO:0000313|EMBL:NDJ89574.1};
GN ORFNames=ACT18_02010 {ECO:0000313|EMBL:OBY33703.1}, BST28_16170
GN {ECO:0000313|EMBL:ORA77937.1}, GWR20_10445
GN {ECO:0000313|EMBL:NDJ89574.1};
OS Mycolicibacter kumamotonensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacter.
OX NCBI_TaxID=354243 {ECO:0000313|EMBL:OBY33703.1, ECO:0000313|Proteomes:UP000092668};
RN [1] {ECO:0000313|EMBL:OBY33703.1, ECO:0000313|Proteomes:UP000092668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Roo {ECO:0000313|EMBL:OBY33703.1,
RC ECO:0000313|Proteomes:UP000092668};
RA Greninger A.L., Cunningham G., Miller S.;
RT "Genome sequence of Mycobacterium kumamotonense strain Roo.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ORA77937.1, ECO:0000313|Proteomes:UP000192713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45093 {ECO:0000313|EMBL:ORA77937.1,
RC ECO:0000313|Proteomes:UP000192713};
RA Tortoli E., Trovato A., Cirillo D.M.;
RT "The new phylogeny of genus Mycobacterium.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:NDJ89574.1, ECO:0000313|Proteomes:UP000466523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CST 7247 {ECO:0000313|EMBL:NDJ89574.1,
RC ECO:0000313|Proteomes:UP000466523};
RA Sanchez-Estrada R., Gonzalez-Y-Merchand J.A., Rivera-Gutierrez S.;
RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
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}.
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:OBY33703.1}.
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DR EMBL; JAACYR010000029; NDJ89574.1; -; Genomic_DNA.
DR EMBL; LFOE01000001; OBY33703.1; -; Genomic_DNA.
DR EMBL; MVHU01000026; ORA77937.1; -; Genomic_DNA.
DR RefSeq; WP_019737095.1; NZ_MVHU01000026.1.
DR AlphaFoldDB; A0A1B8SLY6; -.
DR STRING; 354243.BST28_16170; -.
DR PATRIC; fig|354243.3.peg.426; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000092668; Unassembled WGS sequence.
DR Proteomes; UP000192713; Unassembled WGS sequence.
DR Proteomes; UP000466523; 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; 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; 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; 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.
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}.
FT DOMAIN 206..447
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 129
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 213
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 244
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 381
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 169
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 449 AA; 48613 MW; 68107DFDD609E62B CRC64;
MSELNPKLHD IYDEVLRRNP GEAEFHQAVF EVLSSLGPVV SKHPQYVDSA VIRRMCEPER
QIIFRVPWLD DNGNVQINRG FRVEFNSALG PYKGGLRFHP SVYLGIIKFL GFEQIFKNSL
TGLPIGGGKG GSDFDPKGRS DNEIMRFCQS FMTELYRHLG EYTDVPAGDI GVGGREIGYL
FGQYKRITNR YESGVLTGKG LTWGGSQVRT EATGYGAVFF ADEILKTAKD SFEGKRAVVS
GSGNVAIYAI EKIHQLGGTV VACSDSSGYI VDEKGIDLEL LKEIKEVKRE RIEAYATTRG
GTTQFVNGGS IWDVPCQIAV PSATQNELDG SHAATLAQNG CKIVAEGANM PCTPEAVKLF
TEAGVTVAPG KAANAGGVAT SALEMQQNAS RDSWSFEYTE QRLAAIMQSI HHRCLVTADE
YGAPGNYVVG ANIAGFIQVA DAMTALGLI
//
