ID F5R975_METUF Unreviewed; 447 AA.
AC F5R975;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=METUNv1_00695 {ECO:0000313|EMBL:EGK72866.1};
OS Methyloversatilis universalis (strain ATCC BAA-1314 / JCM 13912 / FAM5).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Sterolibacteriaceae; Methyloversatilis.
OX NCBI_TaxID=1000565 {ECO:0000313|EMBL:EGK72866.1, ECO:0000313|Proteomes:UP000005019};
RN [1] {ECO:0000313|EMBL:EGK72866.1, ECO:0000313|Proteomes:UP000005019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1314 / JCM 13912 / FAM5
RC {ECO:0000313|Proteomes:UP000005019};
RX PubMed=21725020; DOI=10.1128/JB.05331-11;
RA Kittichotirat W., Good N.M., Hall R., Bringel F., Lajus A., Medigue C.,
RA Smalley N.E., Beck D., Bumgarner R., Vuilleumier S., Kalyuzhnaya M.G.;
RT "Genome sequence of Methyloversatilis universalis FAM5T, a methylotrophic
RT representative of the order Rhodocyclales.";
RL J. Bacteriol. 193:4541-4542(2011).
CC -!- SUBUNIT: Homohexamer. {ECO:0000256|ARBA:ARBA00011643}.
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:EGK72866.1}.
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DR EMBL; AFHG01000030; EGK72866.1; -; Genomic_DNA.
DR RefSeq; WP_008058851.1; NZ_AFHG01000030.1.
DR AlphaFoldDB; F5R975; -.
DR STRING; 1000565.METUNv1_00695; -.
DR eggNOG; COG0334; Bacteria.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000005019; 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 CDD; cd05313; NAD_bind_2_Glu_DH; 1.
DR Gene3D; 1.10.285.10; Glutamate Dehydrogenase, chain A, domain 3; 2.
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; 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 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:UP000005019}.
FT DOMAIN 203..445
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 127
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 210
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 241
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 379
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 167
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 447 AA; 48276 MW; 6B047278AAE88F16 CRC64;
MKYGNFSDFV ARVDARNPGQ PEFIQAVTEV MESLWPFIEA NPRYAEQALL ERLVEPERVI
MFRVCWVDDR GEVQVNRGYR IQHSSAIGPY KGGIRFHPSV NLSILKFLAF EQTFKNALTT
LPMGGGKGGS DFDPKGRSQG EIMRFCQAFV SELFRHIGSD TDVPAGDIGV GGREVGYMAG
MMKKLSNRAD CVFTGKGLSF GGSLIRPEAT GYGTVYFAEE MLCHAGRSMA GLRVSVSGSG
NVAQYAVEKA MALGAKVVTV SDSGGTVIDE DGFTTEKLAI LMDVKNRQYG RASDYAKQVG
ARFEENVRPW HVPVDVALPC ATQNELDESD ARTLIANGVK CVAEGANMPS TIEAAKAFEA
AGVLYAPGKA SNAGGVATSG LEMSQNAIRM NWTRDEVDTR LLQIMQGIHA ACLQYGKRKD
GRLSYVDGAN VAGFVKVAEA MLGQGVI
//
