ID A0A2U2CMD4_9RHOB Unreviewed; 368 AA.
AC A0A2U2CMD4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=DDZ14_08025 {ECO:0000313|EMBL:PWE33025.1};
OS Maritimibacter sp. 55A14.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Maritimibacter.
OX NCBI_TaxID=2174844 {ECO:0000313|EMBL:PWE33025.1, ECO:0000313|Proteomes:UP000245064};
RN [1] {ECO:0000313|EMBL:PWE33025.1, ECO:0000313|Proteomes:UP000245064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=55A14 {ECO:0000313|EMBL:PWE33025.1,
RC ECO:0000313|Proteomes:UP000245064};
RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA Wayne K.J., Tettelin H., Glass J.I., Rusch D., Podicherti R., Tsui H.-C.T.,
RA Winkler M.E.;
RL Submitted (MAY-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWE33025.1}.
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DR EMBL; QEYE01000007; PWE33025.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2CMD4; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000245064; Unassembled WGS sequence.
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:UP000245064}.
FT DOMAIN 140..366
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 77
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 149
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 113
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 368 AA; 37822 MW; 7A7D8E4D7AD47859 CRC64;
MATIFEMADD LGPEKVLHVS NPGAGLRAIV VLDNTAAGPA IGGVRMAPDA TLEECARLAR
AMSLKNAAAG LPNGGGKSVI VADPAMPPDA KESVIRAFAE AIAPLSGYIP GPDMGTNETC
MAWVQDEIGR AVGLPRVVGG IPLDEIGATG YGVAVAAAVA EEFCDVPLDG ARVAIQGYGA
VGRHAARCLA EHGARIVAVA DSHGSAFAPD GFDLVRLDAI KADGRSVTDY PGADAGDRKA
VIVAECDILV PAARPDAIDS SNTGAIKARL VVEGANIPAT AESEAALHER GVLVIPDFIA
NAGGVICGSV EYRGGTESQA LAVITERIRH NTREVFQRVN ADGVLPRDAA NSLAEARLRQ
AMALRRSF
//
