ID A0A0C1V717_9ENTR Unreviewed; 447 AA.
AC A0A0C1V717;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=P689_119190 {ECO:0000313|EMBL:KIE64219.1};
OS Candidatus Riesia pediculischaeffi PTSU.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Candidatus Riesia.
OX NCBI_TaxID=1401651 {ECO:0000313|EMBL:KIE64219.1, ECO:0000313|Proteomes:UP000054529};
RN [1] {ECO:0000313|EMBL:KIE64219.1, ECO:0000313|Proteomes:UP000054529}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PTSU {ECO:0000313|EMBL:KIE64219.1,
RC ECO:0000313|Proteomes:UP000054529};
RX PubMed=25213693; DOI=10.1534/g3.114.012567;
RA Boyd B.M., Allen J.M., de Crecy-Lagard V., Reed D.L.;
RT "Genome sequence of Candidatus Riesia pediculischaeffi, endosymbiont of
RT chimpanzee lice, and genomic comparison of recently acquired endosymbionts
RT from human and chimpanzee lice.";
RL G3 (Bethesda) 4:2189-2195(2014).
CC -!- FUNCTION: Catalyzes the reversible oxidative deamination of glutamate
CC to alpha-ketoglutarate and ammonia. {ECO:0000256|ARBA:ARBA00003868}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH +
CC NH4(+); Xref=Rhea:RHEA:11612, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.4.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00001463};
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:KIE64219.1}.
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DR EMBL; AWXV01000002; KIE64219.1; -; Genomic_DNA.
DR RefSeq; WP_039719570.1; NZ_AWXV01000002.1.
DR AlphaFoldDB; A0A0C1V717; -.
DR PATRIC; fig|1401651.3.peg.215; -.
DR HOGENOM; CLU_025763_2_1_6; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000054529; 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 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; IPR014362; Glu_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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.
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 203..444
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 127
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 91
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 115
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 210
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 241
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 379
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 167
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 447 AA; 50007 MW; B25F73907D7FBC96 CRC64;
MKDFLLSNFL NSFSVKYKYQ PEFHQSVKKF LLSISSFLQD NSQYQDVSLL TRLTEPERII
QFRICWMDDL GDIQVNTGWR VQFNSAIGPF KGGIRFHQSV NTSILKFLAF EQTFKNALTN
FPIGGGKGGS DFNPKGKSKM EITRFCQSFV LNLYKYLGTN VDIPAGDIGV SHFEIDLMVG
MMKKILGDSS CVFTGKGLSI FGSQLRKEST GYGVIYFTEL VLNYHNRSIK GKKISISGSG
NVAIYAIEKC IEFGAKVITA SDSNGTVVDL DGFNLEKLNR LKTIKNEIRG RIQQYASELN
LTYLKNQSPW SIPSDIAIPC ATQNEIDEID AKLMIKNDVQ MIVEGSNMPV TEKAIHLFEL
ANILFIPGKI ANSGGVIVSI LEKVQNSTYS VWKRNKVEKK LKEVIKNTHK MCVEYGKKKS
TVDYVKGANI AAFVKVAEAM ISQGMIN
//