GenomeNet

Database: UniProt
Entry: K9JM95_STRUB
LinkDB: K9JM95_STRUB
Original site: K9JM95_STRUB 
ID   K9JM95_STRUB            Unreviewed;       202 AA.
AC   K9JM95;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=NADP-specific glutamate dehydrogenase {ECO:0000313|EMBL:ADU88507.1};
DE   Flags: Fragment;
GN   Name=gdh {ECO:0000313|EMBL:ADU88507.1};
OS   Streptococcus uberis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1349 {ECO:0000313|EMBL:ADU88507.1};
RN   [1] {ECO:0000313|EMBL:ADU88507.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FSL S3-301 {ECO:0000313|EMBL:ADU88493.1}, FSL S3-304
RC   {ECO:0000313|EMBL:ADU88494.1}, FSL S3-423
RC   {ECO:0000313|EMBL:ADU88473.1}, FSL S3-451
RC   {ECO:0000313|EMBL:ADU88496.1}, FSL S3-457
RC   {ECO:0000313|EMBL:ADU88497.1}, FSL Z1-041
RC   {ECO:0000313|EMBL:ADU88507.1}, FSL Z1-276
RC   {ECO:0000313|EMBL:ADU88522.1}, FSL Z2-003
RC   {ECO:0000313|EMBL:ADU88529.1}, FSL Z3-004
RC   {ECO:0000313|EMBL:ADU88549.1}, FSL Z3-333
RC   {ECO:0000313|EMBL:ADU88414.1}, FSL Z3-334
RC   {ECO:0000313|EMBL:ADU88439.1}, FSL Z3-363
RC   {ECO:0000313|EMBL:ADU88435.1}, QMP B5-001
RC   {ECO:0000313|EMBL:ADU88478.1}, QMP B5-005
RC   {ECO:0000313|EMBL:ADU88479.1}, QMP B5-104
RC   {ECO:0000313|EMBL:ADU88481.1}, QMP B5-105
RC   {ECO:0000313|EMBL:ADU88431.1}, and QMP Z3-539
RC   {ECO:0000313|EMBL:ADU88464.1};
RA   Lang P., Stanhope M.;
RT   "Population genetics of Streptococcus uberis using an extended MLST
RT   scheme.";
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|RuleBase:RU004417}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GU434974; ADU88414.1; -; Genomic_DNA.
DR   EMBL; GU434991; ADU88431.1; -; Genomic_DNA.
DR   EMBL; GU434995; ADU88435.1; -; Genomic_DNA.
DR   EMBL; GU434999; ADU88439.1; -; Genomic_DNA.
DR   EMBL; GU435024; ADU88464.1; -; Genomic_DNA.
DR   EMBL; GU435033; ADU88473.1; -; Genomic_DNA.
DR   EMBL; GU435038; ADU88478.1; -; Genomic_DNA.
DR   EMBL; GU435039; ADU88479.1; -; Genomic_DNA.
DR   EMBL; GU435041; ADU88481.1; -; Genomic_DNA.
DR   EMBL; GU435053; ADU88493.1; -; Genomic_DNA.
DR   EMBL; GU435054; ADU88494.1; -; Genomic_DNA.
DR   EMBL; GU435056; ADU88496.1; -; Genomic_DNA.
DR   EMBL; GU435057; ADU88497.1; -; Genomic_DNA.
DR   EMBL; GU435067; ADU88507.1; -; Genomic_DNA.
DR   EMBL; GU435082; ADU88522.1; -; Genomic_DNA.
DR   EMBL; GU435089; ADU88529.1; -; Genomic_DNA.
DR   EMBL; GU435109; ADU88549.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9JM95; -.
DR   GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProt.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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; IPR036291; NAD(P)-bd_dom_sf.
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   PRINTS; PR00082; GLFDHDRGNASE.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU004417}.
FT   DOMAIN          1..78
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02812"
FT   DOMAIN          95..198
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00208"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADU88507.1"
FT   NON_TER         202
FT                   /evidence="ECO:0000313|EMBL:ADU88507.1"
SQ   SEQUENCE   202 AA;  21848 MW;  1A77629F85B01A3C CRC64;
     FLGFEQILKN SLTGQPIGGG KGGSNFDPKG KSDQEVMRFT QSFMTELQKY IGPDLDVPAG
     DIGVGAREIG YLFGQYKRLN GYQNGVLTGK GLTYGGSLVR TEATGYGVVY FAEQMLKSVG
     ESFTGKRAIV SGSGNVAIYA IEKLQELGAV VVAASDSSGY IYDEEGINLK TLKWIKEENR
     NRISTYLEKH PNATFISSDT GK
//
DBGET integrated database retrieval system