ID I0AGA3_IGNAJ Unreviewed; 415 AA.
AC I0AGA3;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN OrderedLocusNames=IALB_0298 {ECO:0000313|EMBL:AFH48010.1};
OS Ignavibacterium album (strain DSM 19864 / JCM 16511 / NBRC 101810 /
OS Mat9-16).
OC Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC Ignavibacteriaceae; Ignavibacterium.
OX NCBI_TaxID=945713 {ECO:0000313|EMBL:AFH48010.1, ECO:0000313|Proteomes:UP000007394};
RN [1] {ECO:0000313|EMBL:AFH48010.1, ECO:0000313|Proteomes:UP000007394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19864 / JCM 16511 / NBRC 101810 / Mat9-16
RC {ECO:0000313|Proteomes:UP000007394};
RX PubMed=22661972; DOI=10.3389/fmicb.2012.00185;
RA Liu Z., Frigaard N.-U., Vogl K., Iino T., Ohkuma M., Overmann J.,
RA Bryant D.A.;
RT "Complete genome of Ignavibacterium album, a metabolically versatile,
RT flagellated, facultative anaerobe from the phylum Chlorobi.";
RL Front. Microbiol. 3:185-185(2012).
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; CP003418; AFH48010.1; -; Genomic_DNA.
DR RefSeq; WP_014559169.1; NC_017464.1.
DR AlphaFoldDB; I0AGA3; -.
DR STRING; 945713.IALB_0298; -.
DR GeneID; 78242056; -.
DR KEGG; ial:IALB_0298; -.
DR PATRIC; fig|945713.3.peg.298; -.
DR eggNOG; COG0334; Bacteria.
DR HOGENOM; CLU_025763_1_2_10; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000007394; 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; 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:SF13; GLUTAMATE DEHYDROGENASE 1, MITOCHONDRIAL; 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:UP000007394}.
FT DOMAIN 182..413
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 105
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 189
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 219
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 145
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 415 AA; 45939 MW; 210F9C420F41066F CRC64;
MESYNSFNVA KQQILEAARL LNLDKATVDL LITPQLETSF TIPVRMDNGD VKIFQAWRIQ
YNNARGPAKG GIRFHPEETV DTIRALACWM TWKTAVVDLP LGGAKGGVRC NPKEMSELEL
ERLSRGYVRA ITPLLGVDVD VPAPDVYTNP QTMAWMMDEY ETIFFKHSPG VFTDKPLQVG
GTEGRRDATA RGGVICVREA CKAYGFDPTK DYAIQGFGNA GQRAALLHQE ILGGGKLVAV
SDSKAAIYNK NGFNPTELVQ HKLKTGSVAN FPGSEKIPHE ELLQLNVEIL YPAALENAIH
SENADKIKAK VVCELANGPT TPEADLILFD KGVHVIPDIL ASAGGVTVSY FEMVQDKTLY
FWDEDEVHRR LDKKMYLAYH RVNEAIKEKK THPRLAAMLV GVARVAQACK LRGWV
//
