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Database: UniProt
Entry: D5UHH3_CELFN
LinkDB: D5UHH3_CELFN
Original site: D5UHH3_CELFN 
ID   D5UHH3_CELFN            Unreviewed;       427 AA.
AC   D5UHH3;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN   OrderedLocusNames=Cfla_2404 {ECO:0000313|EMBL:ADG75294.1};
OS   Cellulomonas flavigena (strain ATCC 482 / DSM 20109 / BCRC 11376 / JCM
OS   18109 / NBRC 3775 / NCIMB 8073 / NRS 134).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=446466 {ECO:0000313|EMBL:ADG75294.1, ECO:0000313|Proteomes:UP000000849};
RN   [1] {ECO:0000313|EMBL:ADG75294.1, ECO:0000313|Proteomes:UP000000849}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 482 / DSM 20109 / BCRC 11376 / JCM 18109 / NBRC 3775 /
RC   NCIMB 8073 / NRS 134 {ECO:0000313|Proteomes:UP000000849};
RX   PubMed=21304688; DOI=10.4056/sigs.1012662;
RA   Abt B., Foster B., Lapidus A., Clum A., Sun H., Pukall R., Lucas S.,
RA   Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Goodwin L., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M.,
RA   Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Cellulomonas flavigena type strain (134).";
RL   Stand. Genomic Sci. 3:15-25(2010).
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; CP001964; ADG75294.1; -; Genomic_DNA.
DR   RefSeq; WP_013117628.1; NC_014151.1.
DR   AlphaFoldDB; D5UHH3; -.
DR   STRING; 446466.Cfla_2404; -.
DR   KEGG; cfl:Cfla_2404; -.
DR   eggNOG; COG0334; Bacteria.
DR   HOGENOM; CLU_025763_1_2_11; -.
DR   OrthoDB; 9803297at2; -.
DR   Proteomes; UP000000849; 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:UP000000849}.
FT   DOMAIN          194..424
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        117
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT   BINDING         81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         105
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         360
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   SITE            157
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ   SEQUENCE   427 AA;  45142 MW;  3A7E8A5627C44D6D CRC64;
     MVADDSPAPA HLEPGAAPLA TAQAQLARAV EILGYDSDLH EVLATPRREL RVAVPLRRDD
     GRVQVFTGYR VQHNISRGPG KGGLRYAPGV DLDEVRALAM WMTWKCAVVD VPYGGAKGGV
     TIDPHAHSSA ELERVTRRYT SEIMPIIGPE RDIMAPDIGT NEQTMAWVMD TYSVNRGFTI
     PAVTTGKPLA VGGSLGRPTA TSQGVVHAAG AALREDGVEL AEVTAAVQGF GKVGSHAARL
     LHESGTRVVA VSDEHGGVRR DGGLDLPALL EHVAATGSVT GFADADPVSN AELLALDVDV
     LVPAAVEGVL DGEAAQRVKA RWVVEGANGP TTSEGDRVLA ERGVVVVPDI LANAGGVVVS
     YFEWVQANQA YWWTEGEIAE RLERRMLASH AAVSALARAE SVTLREAAMT IGVRRVAEAH
     LIRGLYP
//
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