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Database: UniProt
Entry: D5ED85_AMICL
LinkDB: D5ED85_AMICL
Original site: D5ED85_AMICL 
ID   D5ED85_AMICL            Unreviewed;       426 AA.
AC   D5ED85;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN   OrderedLocusNames=Amico_0374 {ECO:0000313|EMBL:ADE56517.1};
OS   Aminobacterium colombiense (strain DSM 12261 / ALA-1).
OC   Bacteria; Synergistota; Synergistia; Synergistales; Aminobacteriaceae;
OC   Aminobacterium.
OX   NCBI_TaxID=572547 {ECO:0000313|EMBL:ADE56517.1, ECO:0000313|Proteomes:UP000002366};
RN   [1] {ECO:0000313|EMBL:ADE56517.1, ECO:0000313|Proteomes:UP000002366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12261 / ALA-1 {ECO:0000313|Proteomes:UP000002366};
RX   PubMed=21304712;
RA   Chertkov O., Sikorski J., Brambilla E., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Lucas S., Tice H., Cheng J.F., Han C.,
RA   Detter J.C., Bruce D., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Spring S.,
RA   Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Aminobacterium colombiense type strain (ALA-
RT   1).";
RL   Stand. Genomic Sci. 2:280-289(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; CP001997; ADE56517.1; -; Genomic_DNA.
DR   RefSeq; WP_013047783.1; NC_014011.1.
DR   AlphaFoldDB; D5ED85; -.
DR   STRING; 572547.Amico_0374; -.
DR   KEGG; aco:Amico_0374; -.
DR   eggNOG; COG0334; Bacteria.
DR   HOGENOM; CLU_025763_1_2_0; -.
DR   OrthoDB; 9803297at2; -.
DR   Proteomes; UP000002366; 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:UP000002366}.
FT   DOMAIN          188..423
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        111
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT   BINDING         75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         195
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         226
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         359
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   SITE            151
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ   SEQUENCE   426 AA;  46568 MW;  B979C7B9F14D1E75 CRC64;
     MSVVKRTSSN VLLDTALKNF YAAAEEMGLE DGLIDILSHS ERKLAVSIPV EMDDGTVKVF
     EGYRVQHSTA IGPAKGGVRF HPEVCLDECE ALSMMMTWKC SLAGIPYGGG KGGVSCDPLE
     MSKREKERVA RTYAARIEPF VDAWTDVPAP DLGTGAPEMV WFMDTISKMR GRLEPAIFTG
     KPIGLWGSKG RTAATGYGVA TCALELFKAL KKDVKGATFA IQGFGNVGTY SAKTLQDAGG
     KVVGISDITG TYYCKDGIDV DKAMNYVQNI HPKRLLEGYE QPGLEKMGLS DILFLDVDLF
     IPAALEGVIN ANNADKVRAK YIVEAANGPL TPEGDAILDE KGVLIVPDFL ANSGGVIGSY
     FEWAQNLSGF FWSIEEYNER LIRIMKDNFA KVWDYSQEKN VKMRRAAFMA AIQRVSDAVR
     MRGVFL
//
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