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Database: UniProt/TrEMBL
Entry: A0A0U2M7H3_9BACL
LinkDB: A0A0U2M7H3_9BACL
Original site: A0A0U2M7H3_9BACL 
ID   A0A0U2M7H3_9BACL        Unreviewed;       458 AA.
AC   A0A0U2M7H3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|ARBA:ARBA00012896, ECO:0000256|PIRNR:PIRNR000185};
GN   ORFNames=IJ22_37740 {ECO:0000313|EMBL:ALS24112.1}, PN4B1_22350
GN   {ECO:0000313|EMBL:GCL72330.1}, SAMN05421868_12045
GN   {ECO:0000313|EMBL:SDJ20508.1};
OS   Paenibacillus naphthalenovorans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=162209 {ECO:0000313|EMBL:ALS24112.1, ECO:0000313|Proteomes:UP000061660};
RN   [1] {ECO:0000313|Proteomes:UP000061660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=32O-Y {ECO:0000313|Proteomes:UP000061660};
RA   Butler R.III., Wang J., Stark B.C., Pombert J.-F.;
RT   "Complete genome sequences of two moderately thermophilic Paenibacillus
RT   species.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ALS24112.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=32O-Y {ECO:0000313|EMBL:ALS24112.1};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ALS24112.1, ECO:0000313|Proteomes:UP000061660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=32O-Y {ECO:0000313|EMBL:ALS24112.1,
RC   ECO:0000313|Proteomes:UP000061660};
RX   PubMed=26868401;
RA   Butler R.R.III., Wang J., Stark B.C., Pombert J.F.;
RT   "Complete Genome Sequences of Two Interactive Moderate Thermophiles,
RT   Paenibacillus napthalenovorans 32O-Y and Paenibacillus sp. 32O-W.";
RL   Genome Announc. 4:e01717-15(2016).
RN   [4] {ECO:0000313|EMBL:SDJ20508.1, ECO:0000313|Proteomes:UP000182184}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR-N1 {ECO:0000313|EMBL:SDJ20508.1,
RC   ECO:0000313|Proteomes:UP000182184};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:GCL72330.1, ECO:0000313|Proteomes:UP000299945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4B1 {ECO:0000313|EMBL:GCL72330.1,
RC   ECO:0000313|Proteomes:UP000299945};
RA   Ha-Thanh L.T., Ngoc-Thi T.V., Shintani M., Moriuchi R., Dohra H.,
RA   Hoang-Loc N., Kimbara K.;
RT   "Isolation and characterization of a moderate thermophilic Paenibacillus
RT   naphthalenovorans strain 4B1 capable of degrading dibenzofuran from dioxin-
RT   contaminated soil in Vietnam.";
RL   Submitted (MAR-2019) 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}.
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DR   EMBL; CP013652; ALS24112.1; -; Genomic_DNA.
DR   EMBL; BJCS01000005; GCL72330.1; -; Genomic_DNA.
DR   EMBL; FNDY01000020; SDJ20508.1; -; Genomic_DNA.
DR   RefSeq; WP_054818182.1; NZ_FNDY01000020.1.
DR   STRING; 162209.IJ22_37740; -.
DR   KEGG; pnp:IJ22_37740; -.
DR   PATRIC; fig|162209.4.peg.4020; -.
DR   OrthoDB; 9803297at2; -.
DR   Proteomes; UP000061660; Chromosome.
DR   Proteomes; UP000182184; Unassembled WGS sequence.
DR   Proteomes; UP000299945; Unassembled WGS sequence.
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; 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:UP000061660}.
FT   DOMAIN          215..456
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        138
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT   BINDING         102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         222
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         253
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         390
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   SITE            178
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ   SEQUENCE   458 AA;  49856 MW;  4C0E7BD3FA89E9E5 CRC64;
     MALETAQHNE LAARTYVNEV YDTVIKRNPH ESEFHQAIKE ILFSLVPVFA KHPKYMQAGI
     LERIVEPERM ITFRVPWVDD QGKVQVNRGF RVQFNSVLGP YKGGLRFHPS VNASIIKFLG
     FEQIFKNSLT GQPIGGGKGG SDFDPKGKSD GEIMRFTQSF MTELFKYIGP DTDVPAGDIG
     VGAREIGYMF GQYRRIRGGN EAGVLTGKGI GYGGSLTRTE ATGYGTVYFV EEMLKSIGLS
     FEDSTVVISG SGNVSLYAIQ KATQLGAKVL ACSDSNGYVY DPDGIKFETV KQIKEVERKR
     ISEYVKEHPN AEYHEGCEGI WTIPCDIALP CATQNEISEA SAKLLVANGV KAVGEGANMP
     STLEAIDVFL ANKVLFGPAK AANAGGVAVS ALEMAQNSMR YSWSFHEVDD KLHAIMKNIY
     RSSVQAAEEY GQPGNLLVGA NIAGFTKVAD AMLAQGII
//
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