ID A0A1M6Q7C1_9CLOT Unreviewed; 455 AA.
AC A0A1M6Q7C1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|ARBA:ARBA00012896, ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=SAMN02745883_01418 {ECO:0000313|EMBL:SHK16048.1};
OS Caminicella sporogenes DSM 14501.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Caminicella.
OX NCBI_TaxID=1121266 {ECO:0000313|EMBL:SHK16048.1, ECO:0000313|Proteomes:UP000184082};
RN [1] {ECO:0000313|EMBL:SHK16048.1, ECO:0000313|Proteomes:UP000184082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14501 {ECO:0000313|EMBL:SHK16048.1,
RC ECO:0000313|Proteomes:UP000184082};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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|PIRNR:PIRNR000185,
CC ECO:0000256|RuleBase:RU004417}.
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DR EMBL; FRAJ01000010; SHK16048.1; -; Genomic_DNA.
DR RefSeq; WP_072966987.1; NZ_FRAJ01000010.1.
DR AlphaFoldDB; A0A1M6Q7C1; -.
DR STRING; 1121266.SAMN02745883_01418; -.
DR Proteomes; UP000184082; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000184082}.
FT DOMAIN 210..453
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 133
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 118
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 172
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 217
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 248
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 173
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 455 AA; 49863 MW; DF6459CF653C9C26 CRC64;
MAGQNLNAKE YIKEVIEKVK ARNASEPEFI QAVEEVLVSL EPVLEKHPEY IEANLLERIT
EPERQIIFRV PWVDDSGKVQ VNRGFRVQFN GAIGPYKGGL RFHPSVYIGI IKFLGFEQIF
KNSLTGLPIG GGKGGSDFDP RGKSDAEIMR FCQSFMTELY RHIGPDVDVP AGDIGVGGRE
IGYLYGQYRR IRGAFENGVL TGKGLAYGGS LIRPEATGFG VTYFAQEMLK HEGETFEGKT
VAISGYGNVA WGVCQKVAEL GGKVVTLSGP DGYIYDPDGV TGEKIDYLVE MLKENKGARV
KDYADKYGVE FFPGEKPWGV KVDIIMPCAI QNDITLEHAK KIVANGIKFV VEGANMPCTN
EAIEYFQKNG VLVGPAKAAN AGGVATSALE MSQNSMRMSW TREEVDKKLH EIMVNIHNNA
MKAAEEYGFG YNLVAGANIA GFLKVAEAMH AQGNY
//
