ID D5AFS8_STRGZ Unreviewed; 448 AA.
AC D5AFS8;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|ARBA:ARBA00012896, ECO:0000256|PIRNR:PIRNR000185};
GN OrderedLocusNames=SSGZ1_0228 {ECO:0000313|EMBL:ADE30693.1};
OS Streptococcus suis (strain GZ1).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=423211 {ECO:0000313|EMBL:ADE30693.1, ECO:0000313|Proteomes:UP000002359};
RN [1] {ECO:0000313|EMBL:ADE30693.1, ECO:0000313|Proteomes:UP000002359}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GZ1 {ECO:0000313|EMBL:ADE30693.1,
RC ECO:0000313|Proteomes:UP000002359};
RX PubMed=19016627; DOI=10.1086/594370;
RA Ye C., Zheng H., Zhang J., Jing H., Wang L., Xiong Y., Wang W., Zhou Z.,
RA Sun Q., Luo X., Du H., Gottschalk M., Xu J.;
RT "Clinical, experimental, and genomic differences between intermediately
RT pathogenic, highly pathogenic, and epidemic Streptococcus suis.";
RL J. Infect. Dis. 199:97-107(2009).
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}.
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DR EMBL; CP000837; ADE30693.1; -; Genomic_DNA.
DR RefSeq; WP_011921833.1; NC_017617.1.
DR AlphaFoldDB; D5AFS8; -.
DR SMR; D5AFS8; -.
DR GeneID; 8154469; -.
DR KEGG; ssw:SSGZ1_0228; -.
DR PATRIC; fig|423211.3.peg.227; -.
DR HOGENOM; CLU_025763_2_1_9; -.
DR Proteomes; UP000002359; Chromosome.
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|PIRNR:PIRNR000185}.
FT DOMAIN 205..446
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 212
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 243
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 380
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 448 AA; 48781 MW; 058D6C24E3BCB26F CRC64;
MSNAKAYIQA SFEAVKARNP HETEFLQAVE ELFSTLEPVF EAHPEYIEEN ILARIVEPER
IISFRVPWTD KDGNVQVNRG YRVQFNSAVG PYKGGLRFHP TVNQSILKFL GFEQIFKNVL
TGLPIGGGKG GSDFDPKGKT DAEIMRFCQS FMTELQKHIG PSLDVPAGDI GVGGREIGYM
YGQYKRLRQF DAGVLTGKPL GFGGSLIRPE ATGYGLVYFT DNMLAANGKS FKDQTVLISG
SGNVAQYAVQ KATELGAKVI SVSDSNGYII DETGIDFDLL VDIKEKRRAR LTEYAAEKST
AKYFKGSVWN YDGKADIALP CATQNEINGK QAAALVKNGV YCVAEGANMP SDLDAIKVYK
ENGVLYGLAK AANAGGVAVS ALEMSQNSLR LSWTREEVDG RLKDIMANIF NTAKETAEKY
DLGTDYLAGA NIAAFEQIAD SMIAQGLV
//
