ID V9W8L1_9BACL Unreviewed; 423 AA.
AC V9W8L1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|ARBA:ARBA00012896, ECO:0000256|PIRNR:PIRNR000185};
GN Name=rocG2 {ECO:0000313|EMBL:AHD06035.1};
GN ORFNames=ERIC2_c22430 {ECO:0000313|EMBL:AHD06035.1};
OS Paenibacillus larvae subsp. larvae DSM 25430.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=697284 {ECO:0000313|EMBL:AHD06035.1, ECO:0000313|Proteomes:UP000029431};
RN [1] {ECO:0000313|EMBL:AHD06035.1, ECO:0000313|Proteomes:UP000029431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25430 {ECO:0000313|EMBL:AHD06035.1,
RC ECO:0000313|Proteomes:UP000029431};
RX PubMed=24599066;
RA Djukic M., Brzuszkiewicz E., Funfhaus A., Voss J., Gollnow K., Poppinga L.,
RA Liesegang H., Garcia-Gonzalez E., Genersch E., Daniel R.;
RT "How to Kill the Honey Bee Larva: Genomic Potential and Virulence
RT Mechanisms of Paenibacillus larvae.";
RL PLoS ONE 9:E90914-E90914(2014).
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}.
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DR EMBL; CP003355; AHD06035.1; -; Genomic_DNA.
DR AlphaFoldDB; V9W8L1; -.
DR KEGG; plv:ERIC2_c22430; -.
DR PATRIC; fig|697284.3.peg.2150; -.
DR eggNOG; COG0334; Bacteria.
DR HOGENOM; CLU_025763_1_2_9; -.
DR Proteomes; UP000029431; Chromosome.
DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
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:UP000029431}.
FT DOMAIN 192..421
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 115
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 199
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 230
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 357
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 155
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 423 AA; 45651 MW; 41AF0FDDDAA52DE7 CRC64;
MSQQTELMQD NENLNSYAIA QKQVEHAASY LGLADHVVEV LKKPMRVLSV SFPVKMDDGS
VKVFEGFRSQ HNNAIGPTKG GIRFHPQVSM DEVKALSMWM SFKCGVVGLP YGGGKGGVIC
DPTEFSQGEL ERISRAFMEA IADIVGPDKD IPAPDVYTNA QVMAWMTDTY SRMKGTFQPG
VITGKPLILG GSLGRNEATA RGCVFTILEA LKDFGKKPSE ATVAVQGFGN AGRIAAELLA
ELGCTIVAVS DSKTALLDLN GLDVTKAAAC KDGGSLATYG SRYEIDPSQI LELDVDILVP
AALENVITLA NADRIQAKVV AEAANGPTTP EADEILFKKG ITVIPDILAN AGGVTVSYFE
WVQNLMNYYW SEEEVNEKLK VTMVKAFAEV QATAKEHNTD LRTGAYIISM KRIAEAMKVR
GWV
//
