ID T5D416_HELPX Unreviewed; 448 AA.
AC T5D416;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=N406_03390 {ECO:0000313|EMBL:EQL63955.1};
OS Helicobacter pylori FD577.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1191283 {ECO:0000313|EMBL:EQL63955.1, ECO:0000313|Proteomes:UP000015967};
RN [1] {ECO:0000313|EMBL:EQL63955.1, ECO:0000313|Proteomes:UP000015967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD577 {ECO:0000313|EMBL:EQL63955.1,
RC ECO:0000313|Proteomes:UP000015967};
RX PubMed=23012278; DOI=10.1128/JB.01278-12;
RA Gunaletchumy S.P., Teh X., Khosravi Y., Ramli N.S., Chua E.G., Kavitha T.,
RA Mason J.N., Lee H.T., Alias H., Zaidan N.Z., Yassin N.B., Tay L.C.,
RA Rudd S., Mitchell H.M., Kaakoush N.O., Loke M.F., Goh K.L., Vadivelu J.;
RT "Draft genome sequences of Helicobacter pylori isolates from Malaysia,
RT cultured from patients with functional dyspepsia and gastric cancer.";
RL J. Bacteriol. 194:5695-5696(2012).
RN [2] {ECO:0000313|EMBL:EQL63955.1, ECO:0000313|Proteomes:UP000015967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD577 {ECO:0000313|EMBL:EQL63955.1,
RC ECO:0000313|Proteomes:UP000015967};
RX PubMed=24051312;
RA Rehvathy V., Tan M.H., Gunaletchumy S.P., Teh X., Wang S., Baybayan P.,
RA Singh S., Ashby M., Kaakoush N.O., Mitchell H.M., Croft L.J., Goh K.L.,
RA Loke M.F., Vadivelu J.;
RT "Multiple genome sequences of Helicobacter pylori strains of diverse
RT disease and antibiotic resistance backgrounds from malaysia.";
RL Genome Announc. 1:E00687-E00713(2013).
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:EQL63955.1}.
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DR EMBL; AKHR02000010; EQL63955.1; -; Genomic_DNA.
DR RefSeq; WP_000275126.1; NZ_AKHR02000010.1.
DR AlphaFoldDB; T5D416; -.
DR PATRIC; fig|1191283.4.peg.1380; -.
DR Proteomes; UP000015967; 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; 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; 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.
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}.
FT DOMAIN 200..447
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 124
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 207
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 238
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 381
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 164
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 448 AA; 49400 MW; C9A82A3BF641D4D4 CRC64;
MYIEKILQSL QKKYPYQKEF HQAVYEAITS LKPLLDSDKS YEKHAILERL IEPEREIFFR
VCWLDDSNQI QVNRGCRVEF NSAIGPYKGG LRFHPSVNES VIKFLGFEQV LKNSLTTLAM
GGAKGGSDFD PKGKSEHEIM RFCQAFMNEL YRHIGATTDV PAGDIGVGER EIGYLFGQYK
KLVNRFEGVL TGKGLTYGGS LCRKEATGYG CVYFAEEMLQ ERNSSLEGKV CSVSGSGNVA
IYTIEKLLQI GAKPVTASDS NGMIYDKDGI DLELLKEIKE VHRGRIKEYA LQKPSAKYTP
TENYPKGGNA VWHVPCFAAF PSATENELSV LDAKTLLSNG CKCVAEGANM PSSNEAIELF
LQAKISYGIG KAANAGGVSV SGLEMAQNAS MHPWSFEVVD AKLHHIMKEI YKNISQTAKE
FKDPTNFVLG ANIAGFRKVA SAMIAQGV
//