ID A0A3D9L8L8_9MICC Unreviewed; 438 AA.
AC A0A3D9L8L8;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=C8E99_0476 {ECO:0000313|EMBL:REE02699.1};
OS Citricoccus muralis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Citricoccus.
OX NCBI_TaxID=169134 {ECO:0000313|EMBL:REE02699.1, ECO:0000313|Proteomes:UP000256727};
RN [1] {ECO:0000313|EMBL:REE02699.1, ECO:0000313|Proteomes:UP000256727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14442 {ECO:0000313|EMBL:REE02699.1,
RC ECO:0000313|Proteomes:UP000256727};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (JUL-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:REE02699.1}.
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DR EMBL; QREH01000001; REE02699.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D9L8L8; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000256727; Unassembled WGS sequence.
DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProt.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000185};
KW Reference proteome {ECO:0000313|Proteomes:UP000256727}.
FT DOMAIN 208..432
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 119
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT SITE 155
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 438 AA; 46042 MW; 7AEEEFC4C17EA301 CRC64;
MTLIQNPDGN RTHDGTSGPA RSARPETLPG TRPETQTGNP AGEPFIRIDP FDRPPEQEIA
WTDPVTGSRG WLVVHTLVGG MATGGTRMRA GCTRDEVADL ARCMATKTAA FGLPVGGAKA
GIDCDPRDPD AMGVLERFFA HMRPWLENSW VTAEDLGVSQ SDLDAVFTRL GLDQSFHAAI
RRSPDPAATL DRVRAGLDTV DQDGLPLGDV IGGYGVAQAC LGTAAAFGWE PTRTTVAIQG
IGTMGGGAAW YLHEAGVPVT AIADAAGTLF CPRGLDIPAL LAARDHYGEI DRATVPSGVE
LLPREAVLAA PADILVPAAV SYALGVGSVA DVAARAVVEA ANSPTTPDAE ERLAVRGIPV
IPDFVANAGA AAWAWWLLQG QVGTDPEDSF RRLREEMQGK VAYMLAEWSG ARVSPRRSAW
GFASANLEAL AGREITIP
//
