ID B7UDW1_STRSU Unreviewed; 418 AA.
AC B7UDW1;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=glutamate dehydrogenase {ECO:0000256|ARBA:ARBA00012896};
DE EC=1.4.1.2 {ECO:0000256|ARBA:ARBA00012896};
DE Flags: Fragment;
OS Streptococcus suis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1307 {ECO:0000313|EMBL:ACK38358.1};
RN [1] {ECO:0000313|EMBL:ACK38358.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WC-SS7 {ECO:0000313|EMBL:ACK38358.1};
RA Cai X.-H., Wang S., Xu M.;
RT "Expression of GDH gene of Streptococcus suis and preparation of monoclonal
RT antibody against GDH.";
RL Submitted (DEC-2008) 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}.
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DR EMBL; FJ517148; ACK38358.1; -; Genomic_DNA.
DR AlphaFoldDB; B7UDW1; -.
DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
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|RuleBase:RU004417}.
FT DOMAIN 175..416
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 99
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 63
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 182
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
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 350
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 139
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACK38358.1"
SQ SEQUENCE 418 AA; 45483 MW; 4F037CA00024544C CRC64;
ELFSTLEPVF EAHPEYIEEN ILARIVEPER IISFRVPWTD KYGNVQVNRG YRVQFNSAVG
PYKGGLRFHP TVNQSILKFL GFEQIFKNVL TGLPIGGGKG GSDFDPKGKT DAEIMRFCQS
FMTELQKHIG PSLDVPAGDI GVGGREIGYM YGQYKRLRQF DAGVLTGKPL GFGGSLIRPE
ATGYGLVYFT DNMLAANGKS FKDQTVLISG SGNVAQYAVQ KATELGAKVI SVSDSNGYII
DETGIDFDLL VDIKEKRRAR LTEYATEKAT AKYFEGSVWN YDGKADIALP CATQNEINGE
QAAALVKNGV YCVAEGANMP SDLDAIKVYK ENGVLYGLAK AANAGGVAVS ALEMSQNSLR
LSWTREEVDG RLKDIMANIF NTAKETAEKY DLGTDYLAGA NIAAFEQIAD SMIAQGLV
//
