ID A0A1L9QQW8_9CYAN Unreviewed; 429 AA.
AC A0A1L9QQW8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=BI308_13570 {ECO:0000313|EMBL:OJJ25064.1};
OS Roseofilum reptotaenium AO1-A.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Desertifilales; Desertifilaceae;
OC Roseofilum.
OX NCBI_TaxID=1925591 {ECO:0000313|EMBL:OJJ25064.1, ECO:0000313|Proteomes:UP000183940};
RN [1] {ECO:0000313|EMBL:OJJ25064.1, ECO:0000313|Proteomes:UP000183940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AO1-A {ECO:0000313|EMBL:OJJ25064.1};
RA Buerger P., Wood-Charlson E.M., Weynberg K.D., Willis B., Van Oppen M.J.;
RT "CRISPR-Cas defence system in Roseofilum reptotaenium: evidence of a
RT bacteriophage-cyanobacterium arms race in the coral black band disease.";
RL Submitted (OCT-2016) 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:OJJ25064.1}.
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DR EMBL; MLAW01000022; OJJ25064.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9QQW8; -.
DR STRING; 1925591.BI308_13570; -.
DR Proteomes; UP000183940; 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; 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:UP000183940}.
FT DOMAIN 195..426
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 118
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 202
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 233
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 158
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 429 AA; 46090 MW; 76FC6552041E592A CRC64;
MMPSSVKMPQ PPTPAHICPM DRTCSYLQQA GSELNIDRGI LTVLENPRKV VTVSIPVKLD
TGEVQVLAGH RVQHCDVLGP YKGGTRYHPS VTLQEVSSLA MLMTWKCALL GIPYGGAKGG
IALDPHQYSV GELERITRRY TSELIKDIGP AVDIPAPDMG TSAREMAWMM DTYSMNVGHA
VPGIVTGKPL SVGGSKGRQQ ATGRGVMIVV REALAQQDKP LAGASVVIQG FGNVGGAAAL
LFHQAGAKVL AVSNVSGAIF AENGLDIPAL RKHVVENHAP MNNFPGGEWI TNEELLTLPC
DVLIPAALED QITEENAPRI QAKIVAEAAN GPVTLVADQL LHSRGIMVLP DILANAGGVV
VSYLEWVQGQ SYVFWDEERV NQEMEGLMVR AYHRVYETSQ QRGIPLRLAA YTLGVGRVAQ
ALSDRGLYP
//
