ID J2PQA1_9PSED Unreviewed; 339 AA.
AC J2PQA1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Glutamate dehydrogenase/leucine dehydrogenase {ECO:0000313|EMBL:EJM25794.1};
GN ORFNames=PMI24_04142 {ECO:0000313|EMBL:EJM25794.1};
OS Pseudomonas sp. GM25.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144327 {ECO:0000313|EMBL:EJM25794.1, ECO:0000313|Proteomes:UP000007510};
RN [1] {ECO:0000313|EMBL:EJM25794.1, ECO:0000313|Proteomes:UP000007510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM25 {ECO:0000313|EMBL:EJM25794.1,
RC ECO:0000313|Proteomes:UP000007510};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
CC -!- FUNCTION: Catalyzes the reversible oxidative deamination of glutamate
CC to alpha-ketoglutarate and ammonia. {ECO:0000256|ARBA:ARBA00003868}.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382, 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:EJM25794.1}.
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DR EMBL; AKJQ01000049; EJM25794.1; -; Genomic_DNA.
DR RefSeq; WP_007957253.1; NZ_AKJQ01000049.1.
DR AlphaFoldDB; J2PQA1; -.
DR PATRIC; fig|1144327.3.peg.4042; -.
DR Proteomes; UP000007510; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR CDD; cd01075; NAD_bind_Leu_Phe_Val_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; IPR016211; Glu/Phe/Leu/Val/Trp_DH_bac/arc.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42722; LEUCINE DEHYDROGENASE; 1.
DR PANTHER; PTHR42722:SF1; VALINE DEHYDROGENASE; 1.
DR Pfam; PF00208; ELFV_dehydrog; 2.
DR Pfam; PF02812; ELFV_dehydrog_N; 1.
DR PIRSF; PIRSF000188; Phe_leu_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:PIRSR000188-2};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000188-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU004417}.
FT DOMAIN 138..339
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT BINDING 174..179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 339 AA; 35676 MW; 36BB004395C5A42F CRC64;
MFALMQSTRL ESLHLSVDPV SGLKAVIAIH NSRLGPALGG CRYLAYPNDE SAVEDAIRLA
QGMSYKAALA GLAQGGGVAV IVRPAHVENR GALFEAFGRC IDQLDGRYIT AIDSGTSVAD
MDCIAQQTQH VTSTTSAGDP APHAAMGVFT GIRATAMARL GSDNLEGLRV AIQGLGNVGY
ALAEQLHAAG AELLVSDIDH GKVQLAMEQL NAHPIANDAL LSTPCDILAP CGLGGVLNSH
SVTQLRCSAV AGSANNQLTH LDVADQLERR GILYAPDYVI NAGGLIYVSL KHRGEELTTI
TAHLSKISSR LTEVFAHAQA EKRSPARVAD ELAEKVLYR
//
