ID J0DH54_9BIFI Unreviewed; 449 AA.
AC J0DH54;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=HMPREF9156_00457 {ECO:0000313|EMBL:EJD65693.1};
OS Scardovia wiggsiae F0424.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Scardovia.
OX NCBI_TaxID=857290 {ECO:0000313|EMBL:EJD65693.1, ECO:0000313|Proteomes:UP000006415};
RN [1] {ECO:0000313|EMBL:EJD65693.1, ECO:0000313|Proteomes:UP000006415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0424 {ECO:0000313|EMBL:EJD65693.1,
RC ECO:0000313|Proteomes:UP000006415};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A.,
RA Baranova O.V., Blanton J.M., Tanner A.C., Mathney J., Dewhirst F.E.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA Alvarado L., Arachchi H.M., Berlin A., Chapman S.B., Gearin G.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D., Howarth C.,
RA Larimer J., Lui A., MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Scardovia wiggsiae F0424.";
RL Submitted (JAN-2012) 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}.
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:EJD65693.1}.
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DR EMBL; AGZS01000001; EJD65693.1; -; Genomic_DNA.
DR RefSeq; WP_007147524.1; NZ_JH719939.1.
DR AlphaFoldDB; J0DH54; -.
DR STRING; 857290.HMPREF9156_00457; -.
DR GeneID; 84815390; -.
DR eggNOG; COG0334; Bacteria.
DR HOGENOM; CLU_025763_2_1_11; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000006415; 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; 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:UP000006415}.
FT DOMAIN 205..447
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 244
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 381
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 449 AA; 49046 MW; 4B59B56C855D1B20 CRC64;
MAFSDPYLER VYQQAERRDG GQQEFLQAVR EVFETLEPVI KAHPEYEANG ILERFIEPER
EIKFRVTWVD DNGRTQVNRG YRVEFNSAIG PYKGGLRFHP TVTESVVKFL GFEQILKNSL
TGLPMGGGKG GSDFDPRGRS DGEVMRFCQA FMTELQRHIG QFTDVPAGDI NVGAREVGYL
FGQYKRIRNE YTGTLTGKGL EFGGSLIRTE ATGYGLCYYT NDAMKELRND SFEGKTVAVS
GSGNVAIFAI EKAQQLGAAA VTASDSDGYV YDPNGIDLDV LKDIKLIERG RISEYAQRVP
GSEYHEGCSG VWEVKCDIAL PCATQNEISE ESAKKLVSNR CTVVCEGANM PSTPAAIAVY
RSNGVLYGPA KAANAGGVAV SGLEMSQNSL RLQWPSEEVD QRLQDIMRGI VSESLAAAHE
YGHDGDLMLG ANIAGFTKVA NAMVAQGVM
//
