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Database: UniProt
Entry: A0A0C1V717_9ENTR
LinkDB: A0A0C1V717_9ENTR
Original site: A0A0C1V717_9ENTR 
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
//
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