ID A0A0Q9ZHW4_9FLAO Unreviewed; 447 AA.
AC A0A0Q9ZHW4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=APR42_08585 {ECO:0000313|EMBL:KRG27800.1};
OS Salegentibacter mishustinae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Salegentibacter.
OX NCBI_TaxID=270918 {ECO:0000313|EMBL:KRG27800.1, ECO:0000313|Proteomes:UP000051643};
RN [1] {ECO:0000313|EMBL:KRG27800.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 12263 {ECO:0000313|EMBL:KRG27800.1};
RA Lin W., Zheng Q.;
RT "Draft genome sequence of Salegentibacter mishustinae KCTC 12263.";
RL Submitted (OCT-2015) 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:KRG27800.1}.
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DR EMBL; LKTP01000034; KRG27800.1; -; Genomic_DNA.
DR RefSeq; WP_057482473.1; NZ_QKZW01000004.1.
DR AlphaFoldDB; A0A0Q9ZHW4; -.
DR STRING; 270918.APR42_08585; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000051643; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000051643}.
FT DOMAIN 202..445
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 126
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 111
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 165
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 209
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 240
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 379
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 166
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 447 AA; 49704 MW; 07B61BFAC1F0C278 CRC64;
MEQNIQDFLD KVSQRNQNEP EFMQAVHEVS ETIIPFIEEN KKYQNMQLLE RMVEPERVIM
FRVSWLDDEG NIQVNRGFRI QMNSAIGPYK GGLRFHPSVN LSILKFLAFE QVFKNSLTTL
PMGGGKGGSD FDPKGKSDNE VMRFCQSFMT ELYRHIGPDT DVPAGDIGVG AREVGYMFGQ
YKRLQNEFTG ILTGKGLSYG GSLIRPEATG YGNVYFAQNM LRTRDESFEG KTVVVSGSGN
VAQYAAEKAL EFGAKILTMS DSGGYIYDEA GIDEEKLQFI MDLKNVRRGR ISEYVDEYSS
AKYFEGETPW GVKCDVALPC ATQNELEEAD AKKLVENGCM CVGEGANMPC TPEAVEVFKE
AKILFSPGKA SNAGGVATSG LEMSQNSMRY SWTSEEVDKK LHEIMNNIHD RCVEFGKEED
GYIDYVKGAN IAGFVKVADA MLAQGVV
//
