ID A1KUS5_NEIMF Unreviewed; 421 AA.
AC A1KUS5;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN OrderedLocusNames=NMC1413 {ECO:0000313|EMBL:CAM10624.1};
OS Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM
OS 15464 / FAM18).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=272831 {ECO:0000313|EMBL:CAM10624.1, ECO:0000313|Proteomes:UP000002286};
RN [1] {ECO:0000313|EMBL:CAM10624.1, ECO:0000313|Proteomes:UP000002286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700532 / DSM 15464 / FAM18
RC {ECO:0000313|Proteomes:UP000002286};
RX PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C.,
RA Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K.,
RA Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S.,
RA Quail M.A., Achtman M., Barrell B., Saunders N.J., Parkhill J.;
RT "Meningococcal genetic variation mechanisms viewed through comparative
RT analysis of serogroup C strain FAM18.";
RL PLoS Genet. 3:230-240(2007).
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; AM421808; CAM10624.1; -; Genomic_DNA.
DR RefSeq; WP_002221776.1; NC_008767.1.
DR AlphaFoldDB; A1KUS5; -.
DR KEGG; nmc:NMC1413; -.
DR HOGENOM; CLU_025763_1_2_4; -.
DR Proteomes; UP000002286; Chromosome.
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; 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}.
FT DOMAIN 188..419
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 111
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 195
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 226
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 355
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 151
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 421 AA; 46111 MW; 29BB10B8C0FFD9F8 CRC64;
MSEALAKETL NPFEIARKQV KTACDRLKTD PAVYEILKSP TRVLEVNFPV KLDDGTVKTF
TGYRSQHNNA VGPYKGGVRF HPGVNLDEVK ALSIWMTIKC CVAGIPYGGG KGGVTLNPRD
YSEAELERIA RAYSEAISPL IGEKIDIPAP DVNTNGKIMS WMVDAYENVV KHSAPGVFTG
KPVEFGGSLA RTEATGYGVN LAAVQALEKL GKDVKGATYA IQGFGNVGYH TGYYAHQSGA
KVVAVSTVDV AIYNENGLDM EAIIKEFQTK GFITNEAGYG KEITNAELLA LEVDVLAPCA
LENQLTSENA GKVRATIVVE GANGPTTPEA DVILRQNGVL VVPDILANCG GVVVSYFEWV
QNLQGYYWEF DEVQEKETVV LRRAFRDIWN LAQEYDVDLR TASYMMSIRR VEKAMKLRGW
Y
//
