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Database: UniProt
Entry: W5W4Q4_9PSEU
LinkDB: W5W4Q4_9PSEU
Original site: W5W4Q4_9PSEU 
ID   W5W4Q4_9PSEU            Unreviewed;       368 AA.
AC   W5W4Q4;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN   ORFNames=KALB_2840 {ECO:0000313|EMBL:AHH96208.1};
OS   Kutzneria albida DSM 43870.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Kutzneria.
OX   NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHH96208.1, ECO:0000313|Proteomes:UP000019225};
RN   [1] {ECO:0000313|EMBL:AHH96208.1, ECO:0000313|Proteomes:UP000019225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43870 {ECO:0000313|EMBL:AHH96208.1};
RX   PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA   Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA   Bechthold A., Kalinowski J., Luzhetskyy A.;
RT   "Complete genome sequence of producer of the glycopeptide antibiotic
RT   Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT   of Pseudonocardiaceae.";
RL   BMC Genomics 15:885-885(2014).
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; CP007155; AHH96208.1; -; Genomic_DNA.
DR   AlphaFoldDB; W5W4Q4; -.
DR   STRING; 1449976.KALB_2840; -.
DR   KEGG; kal:KALB_2840; -.
DR   PATRIC; fig|1449976.3.peg.2853; -.
DR   eggNOG; COG0334; Bacteria.
DR   HOGENOM; CLU_025763_1_1_11; -.
DR   Proteomes; UP000019225; 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   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   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:UP000019225}.
FT   DOMAIN          136..362
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        70
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT   BINDING         34
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         58
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         145
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   SITE            106
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ   SEQUENCE   368 AA;  38411 MW;  A70DF12A74893F1A CRC64;
     MDEWGPEKVV CVSDTRTGMR GVLVIDNTAR GMGKGGTRMS PGLTVAEVAR LARVMTWKWA
     GVDLFHGGAK AGIRFDPARA DKEAVLRAFV RALSNEVPAE YVLGLDVGMT ERDAAVVQDE
     LRDRGAAVGT PAELGGVPYD QLGVTGYGLA EATDAVTELT GARVAIQGFG AVGRAAAKRY
     AELGATVVAV SSALGVRHDP DGLDVAALLA VPGDRTVTEY RGGRLLALGE ELLVPAEVLV
     PAATQDVIDV DLAGRIGARV VVEGANLPTT PAAQRVLATR GVTVLPDFIA NAGGVVAAAY
     AMDARYSALR PDPAAIYAVI ADKLRANAVT VLDHARALGR TTHEAARDLA QTRVREAMRL
     RGRLPNPS
//
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