ID E6X2G0_NITSE Unreviewed; 453 AA.
AC E6X2G0;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN OrderedLocusNames=Nitsa_1921 {ECO:0000313|EMBL:ADV47165.1};
OS Nitratifractor salsuginis (strain DSM 16511 / JCM 12458 / E9I37-1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurovaceae; Nitratifractor.
OX NCBI_TaxID=749222 {ECO:0000313|EMBL:ADV47165.1, ECO:0000313|Proteomes:UP000008633};
RN [1] {ECO:0000313|EMBL:ADV47165.1, ECO:0000313|Proteomes:UP000008633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16511 / JCM 12458 / E9I37-1
RC {ECO:0000313|Proteomes:UP000008633};
RX PubMed=21886859;
RA Anderson I., Sikorski J., Zeytun A., Nolan M., Lapidus A., Lucas S.,
RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L.,
RA Pitluck S., Liolios K., Pagani I., Ivanova N., Huntemann M., Mavromatis K.,
RA Ovchinikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Brambilla E.M., Ngatchou-Djao O.D., Rohde M., Tindall B.J., Goker M.,
RA Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Nitratifractor salsuginis type strain (E9I37-
RT 1).";
RL Stand. Genomic Sci. 4:322-330(2011).
RN [2] {ECO:0000313|Proteomes:UP000008633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16511 / JCM 12458 / E9I37-1
RC {ECO:0000313|Proteomes:UP000008633};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Zeytun A.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Schuetze A.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Nitratifractor salsuginis DSM 16511.";
RL Submitted (JAN-2011) 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; CP002452; ADV47165.1; -; Genomic_DNA.
DR RefSeq; WP_013554850.1; NC_014935.1.
DR AlphaFoldDB; E6X2G0; -.
DR STRING; 749222.Nitsa_1921; -.
DR KEGG; nsa:Nitsa_1921; -.
DR eggNOG; COG0334; Bacteria.
DR HOGENOM; CLU_025763_2_1_7; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000008633; Chromosome.
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:UP000008633}.
FT DOMAIN 204..451
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 128
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 211
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 242
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 385
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 168
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 453 AA; 49425 MW; 6F154FDFB1542ACA CRC64;
MSAKEYIDDV LKFIRECSPG QNEFYQAATE VFESLTPLLE EEEKYRDYAI LERIVQPERT
IIFRVTWIDD AGKIQTNLGY RVQFNSTLGP YKGGLRFHPT VNLGIIKFLG FEQIFKNALT
GLGIGGGKGG SNFDPKGKSD AEVNRFCQAF MNELYRHIGT TRDVPAGDIG VGAREIGYLF
GQYKLLTASF EGAMTGKGVG WGGSFGRREA TGYGSVYFAE HILNSHGDEL KGKTCCVSGA
GNVAIYTIEK LKSMGATPVT CSDSRGTIHH PKGIDVKTLK AIKEVSRESL EKYAQLHPDA
TYIPIHKYPE GGHAVWSIPC DVAFPSATQN ELTLVDAKNL VKNGCKLVNE GANMPTTPDA
LEYLRKHGVL FGPAKAANAG GVAVSQLEMA QNASMQRWSF AEVDTKLFGI MKSIFETADE
TAREFGHEGD LLMGANIAGF RRVADAMIDE GAV
//
