ID C5EXX2_9HELI Unreviewed; 451 AA.
AC C5EXX2;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN Name=gdhA {ECO:0000313|EMBL:EEQ62742.1};
GN ORFNames=HPMG_00199 {ECO:0000313|EMBL:EEQ62742.1};
OS Helicobacter pullorum MIT 98-5489.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=537972 {ECO:0000313|EMBL:EEQ62742.1};
RN [1] {ECO:0000313|EMBL:EEQ62742.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MIT 98-5489 {ECO:0000313|EMBL:EEQ62742.1};
RG The Broad Institute Genome Sequencing Platform;
RA Fox J.G., Shen Z., Charoenlap N., Schauer D.B., Ward D., Mehta T.,
RA Young S., Jaffe D., Gnerre S., Berlin A., Heiman D., Hepburn T., Shea T.,
RA Sykes S., Alvarado L., Kodira C., Borodovsky M., Lander E., Galagan J.,
RA Nusbaum C., Birren B.;
RT "Annotation of Helicobacter pullorum strain MIT 98-5489.";
RL Submitted (AUG-2008) 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; DS990441; EEQ62742.1; -; Genomic_DNA.
DR RefSeq; WP_005020708.1; NZ_DS990441.1.
DR AlphaFoldDB; C5EXX2; -.
DR eggNOG; COG0334; Bacteria.
DR HOGENOM; CLU_025763_2_1_7; -.
DR Proteomes; UP000003953; 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 201..449
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 125
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 208
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 240
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 383
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 165
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 451 AA; 49671 MW; 4BACF60537B2BC17 CRC64;
MSYTQSVIQK VQKLYPDQVE FHQAVKEVLE SIEPALQKDK RYEKYKVLER IVIPERQINF
RVTWEDDKGE IQVNRGYRIE FSSLLGPYKG GLRFHPSVTE GIIKFLGFEQ IFKNSLTGLA
MGGGKGGSDF DPKGKSDREV MRFCQAFMNE LYRHIGAHTD VPAGDIGVGG REIGYLFGQY
KKLTNRYDGV LTGKSLLWGG SLVRTEATGY GSVYFAQEML KHSDFGSLEG KTCLVSGSGN
VAIYTIEKLQ QLGAKPVTIS DSKGIIYDES GIDLALLKEI KEVRRESLES YAKEKPSAKY
TSTRDYPSDH NPLWAIPAFA AFPSATQNEI NAKDAENLLK NGCKCVSEGA NMPSTIEAVH
KFLDAKICYG PGKAANAGGV ATSGLEMSQN ASMTAWSFEE VDSKLHKIMQ NIYANASQTA
KEFGEPTNLV LGANIAGFRK VANAMIEQGL V
//
