ID A0A1R1L6H6_9MICC Unreviewed; 446 AA.
AC A0A1R1L6H6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=BKD30_14805 {ECO:0000313|EMBL:OMH23123.1};
OS Tersicoccus phoenicis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Tersicoccus.
OX NCBI_TaxID=554083 {ECO:0000313|EMBL:OMH23123.1, ECO:0000313|Proteomes:UP000187085};
RN [1] {ECO:0000313|EMBL:OMH23123.1, ECO:0000313|Proteomes:UP000187085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1p05MA {ECO:0000313|EMBL:OMH23123.1,
RC ECO:0000313|Proteomes:UP000187085};
RA Nakajima Y., Yoshizawa S., Nakamura K., Ogura Y., Hayashi T., Kogure K.;
RT "Draft genome of Tersicoccus phoenicis 1P05MA.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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:OMH23123.1}.
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DR EMBL; MRDE01000081; OMH23123.1; -; Genomic_DNA.
DR RefSeq; WP_076705814.1; NZ_MRDE01000081.1.
DR AlphaFoldDB; A0A1R1L6H6; -.
DR STRING; 554083.BKD30_14805; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000187085; 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; 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.
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:UP000187085}.
FT DOMAIN 206..444
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 129
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 213
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 244
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 378
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 169
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 446 AA; 48122 MW; 65A6AA44C93EE0B0 CRC64;
MPAAEAALHD VYTEVLQRNP GESEFHQAVH EVLDSLAPVV RKHPEYLDAA VFSRICEPER
QIIFRVPWID DAGAVRLNRG FRVQFNSALG PYKGGLRFHP SVNLGIVKFL GFEQIFKNSL
TGMPIGGGKG GSDFDPKGKS DREVMRFCQS LMTELNRHIG AEVDVPAGDI GVGTREIGYL
FGQYKRLANR YESGALTGKG LTWGGSQVRT EATGYGTVYF AQEMLRARGE SFDGKRVVVS
GSGNVAIYAI EKVHEFGGTV VACSDSSGYV VDEAGIDLDL LKEVKEVRRE RIDAYTEHRG
RLVADGSIWE VPCDIALPSA TQNELQEADA IALVRSGCRY VAEGANMPTT PDAVRVLTDA
GVAFGPGKAA NAGGVATSAL EMQQNASRDS WSFEYTEDRL AGIMREIHDS CATTADEFGS
PGNYVVGANI AGFLRVADAM VALGVI
//
