ID A0A1J6Y4V9_9MICO Unreviewed; 430 AA.
AC A0A1J6Y4V9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Glutamate dehydrogenase {ECO:0000313|EMBL:OIU85425.1};
DE Flags: Fragment;
GN ORFNames=BFN01_12420 {ECO:0000313|EMBL:OIU85425.1};
OS Microbacterium sp. AR7-10.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1891970 {ECO:0000313|EMBL:OIU85425.1, ECO:0000313|Proteomes:UP000183831};
RN [1] {ECO:0000313|EMBL:OIU85425.1, ECO:0000313|Proteomes:UP000183831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR7-10 {ECO:0000313|EMBL:OIU85425.1,
RC ECO:0000313|Proteomes:UP000183831};
RA Pei D., Jiang J., Chen H., Li K., Yu W., Ma Y., Xu J.;
RT "The draft genome of Microbacterium sp. AR7-10 isolated from the wild
RT caught mosquito Anopheles.";
RL Submitted (SEP-2016) 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|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:OIU85425.1}.
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DR EMBL; MJIR01000087; OIU85425.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J6Y4V9; -.
DR STRING; 1891970.BFN01_12420; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000183831; 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 Gene3D; 1.10.285.10; Glutamate Dehydrogenase, chain A, domain 3; 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; IPR014362; Glu_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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|RuleBase:RU004417}.
FT DOMAIN 213..429
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 136
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 220
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 251
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 387
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 176
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
FT NON_TER 430
FT /evidence="ECO:0000313|EMBL:OIU85425.1"
SQ SEQUENCE 430 AA; 46685 MW; 6E93629987B38355 CRC64;
MTENTADFHP LSDAAQPVFD TVRSLNPNEP EFHQAVHEVL HSIGPVLERH PKYLDQGVLE
RLVEPERQVI FRVPWIDDAG KLQVNRGYRV QYNSALGPYK GGLRFHPSVN ISIIKFLGFE
QIFKNALTGQ GIGGGKGGSN FDPHGKSEAE VMRFCQSFMS ELFRHIGEHT DVPAGDIGVG
GREIGYLFGM YRKMTNRHES GILTGKGIGW GGAQVRTEAT GYGAVFFVQE MLAVHGESLE
GKRVAVSGSG NVAIYAIEKA TQLGARAITA SDSSGYIVDD AGIDLALLRQ IKEVERARIV
EYANRRPGAR FVEGGNVWET PVDIAVPSAT QNELNEDSAR MLIANGVRAV AEGANMPSTP
EAVGAFQDSE VLFAPGKAAN AGGVATSALE MSQNASRQRW NFANSEQKLR DIMADIHDAS
FRAAERYGTP
//
