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Database: UniProt
Entry: T5D416_HELPX
LinkDB: T5D416_HELPX
Original site: T5D416_HELPX 
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
//
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