ID A0A2S7TXB5_9BACT Unreviewed; 416 AA.
AC A0A2S7TXB5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=BSZ32_01885 {ECO:0000313|EMBL:PQJ27368.1};
OS Rubritalea profundi.
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC Rubritaleaceae; Rubritalea.
OX NCBI_TaxID=1658618 {ECO:0000313|EMBL:PQJ27368.1, ECO:0000313|Proteomes:UP000239907};
RN [1] {ECO:0000313|EMBL:PQJ27368.1, ECO:0000313|Proteomes:UP000239907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAORIC-165 {ECO:0000313|EMBL:PQJ27368.1,
RC ECO:0000313|Proteomes:UP000239907};
RA Song J., Yoshizawa S., Kogure K.;
RT "Study of bacterial adaptation to deep sea.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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:PQJ27368.1}.
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DR EMBL; MQWA01000001; PQJ27368.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7TXB5; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000239907; 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; cd01076; NAD_bind_1_Glu_DH; 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; 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; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11606:SF24; GLUTAMATE DEHYDROGENASE 2; 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:UP000239907}.
FT DOMAIN 176..406
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 100
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 183
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 214
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 342
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 140
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 416 AA; 45100 MW; 1A4CDEAEF0CDC17C CRC64;
MLQDVHQFFQ KAADILDLSD CIRKILLTPR RIVKVEIITE SDDGNLMHHM GFRVQHNNAR
GPMKGGLRYH PSMDEEHATA LASLMTWKTA VVDIPFGGAK GGINCDPRAL STSELSAITR
SFVGRIKEVI GPTIDIPAPD VNTNAEIMGW IMDEYSRHYG FSPGVVTGKP LHLFGSEGRE
DATGRGVLYV LQEVLRQQGR ELKGMKVAVQ GFGNVGSHAA RLMADAGAII VAVADHTGGT
SRDTGLDIAK LIDWSKSHGG IAGFEGGDAF DGTLIATFDC DVFVPAALEN VINQDNVDEV
RANYIVEGAN GPTSADASSQ LTERGVTIIP DILANAGGVT ASYFEWVQNI QQFRWDRERV
NQELHKVMTR STNDVIEAAA HYSTDLRTAA FVLAIKRVGK ASAARVHIRE NIAGLD
//
