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Database: UniProt
Entry: H8KV07_SOLCM
LinkDB: H8KV07_SOLCM
Original site: H8KV07_SOLCM 
ID   H8KV07_SOLCM            Unreviewed;       478 AA.
AC   H8KV07;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN   OrderedLocusNames=Solca_0892 {ECO:0000313|EMBL:AFD06007.1};
OS   Solitalea canadensis (strain ATCC 29591 / DSM 3403 / NBRC 15130 / NCIMB
OS   12057 / USAM 9D) (Flexibacter canadensis).
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Solitalea.
OX   NCBI_TaxID=929556 {ECO:0000313|EMBL:AFD06007.1, ECO:0000313|Proteomes:UP000007590};
RN   [1] {ECO:0000313|Proteomes:UP000007590}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29591 / DSM 3403 / NBRC 15130 / NCIMB 12057 / USAM 9D
RC   {ECO:0000313|Proteomes:UP000007590};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Lu M.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Spring S., Schroeder M., Kopitz M., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Solitalea canadensis DSM 3403.";
RL   Submitted (FEB-2012) 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}.
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DR   EMBL; CP003349; AFD06007.1; -; Genomic_DNA.
DR   RefSeq; WP_014679235.1; NC_017770.1.
DR   AlphaFoldDB; H8KV07; -.
DR   STRING; 929556.Solca_0892; -.
DR   KEGG; scn:Solca_0892; -.
DR   eggNOG; COG0334; Bacteria.
DR   HOGENOM; CLU_025763_1_0_10; -.
DR   OrthoDB; 9803297at2; -.
DR   Proteomes; UP000007590; 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:UP000007590}.
FT   DOMAIN          194..475
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        113
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT   BINDING         77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         201
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         240
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         369
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   SITE            155
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ   SEQUENCE   478 AA;  52838 MW;  9AD98EA13D484088 CRC64;
     MAKKPSKAAA HEISFWDDVC DYFNHAATFT DHPKDILEMI RECNSIYSFK FPIRANGGFE
     LISAWRVEHS HHKLPTKGGI RYSEFVHEDE VKALAALMTY KCAIVNVPYG GAKGGVKVNP
     KKYSERELEN ITRRYTSELI KKNFIGPGTD VPAPDYGTGE REMSWIVDTY QAYNPGQIDS
     NACVTGKPLA QHGIAGRREA TGRGVFFAAR ECVNVPEDMK KVKLSVGLEG KRVIVQGLGN
     VGYYSAKFIQ EAGGIIVGLC EYEGAIYDSK GLDVDDVVRH RKETGSILNY KKAKNFKNSS
     EGLEQECDIF VPAALENQIH DGNIAAIKAK IIVEGANGPT TPDAATAFIK RGGIIVPDMY
     ANAGGVTVSY FEWLKNLSHV AFGRMNKRFE ENAARNMVDM IERMTGQSIT ADQRTVIVKG
     ASELELVNSG LEETMVRAYH EIRDIQLANK KITDLRMAAF VCAIDKVAIS YKNLGIFP
//
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