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Database: UniProt
Entry: Q930S3_RHIME
LinkDB: Q930S3_RHIME
Original site: Q930S3_RHIME 
ID   Q930S3_RHIME            Unreviewed;       448 AA.
AC   Q930S3;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 110.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN   Name=gdhA {ECO:0000313|EMBL:AAK64780.1};
GN   ORFNames=SMa0228 {ECO:0000313|EMBL:AAK64780.1};
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OG   Plasmid pSymA {ECO:0000313|EMBL:AAK64780.1,
OG   ECO:0000313|Proteomes:UP000001976}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834 {ECO:0000313|EMBL:AAK64780.1, ECO:0000313|Proteomes:UP000001976};
RN   [1] {ECO:0000313|EMBL:AAK64780.1, ECO:0000313|Proteomes:UP000001976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021 {ECO:0000313|EMBL:AAK64780.1,
RC   ECO:0000313|Proteomes:UP000001976};
RC   PLASMID=Plasmid pSymA {ECO:0000313|Proteomes:UP000001976};
RX   PubMed=11481432; DOI=10.1073/pnas.161294798;
RA   Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F.,
RA   Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L.,
RA   Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H., Palm C.,
RA   Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A.,
RA   Long S.R.;
RT   "Nucleotide sequence and predicted functions of the entire Sinorhizobium
RT   meliloti pSymA megaplasmid.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001).
RN   [2] {ECO:0000313|Proteomes:UP000001976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021 {ECO:0000313|Proteomes:UP000001976};
RC   PLASMID=Plasmid pSymA {ECO:0000313|Proteomes:UP000001976};
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
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; AE006469; AAK64780.1; -; Genomic_DNA.
DR   PIR; B95277; B95277.
DR   RefSeq; NP_435368.1; NC_003037.1.
DR   RefSeq; WP_010967123.1; NC_003037.1.
DR   AlphaFoldDB; Q930S3; -.
DR   EnsemblBacteria; AAK64780; AAK64780; SMa0228.
DR   GeneID; 61598968; -.
DR   KEGG; sme:SMa0228; -.
DR   PATRIC; fig|266834.11.peg.126; -.
DR   HOGENOM; CLU_025763_2_1_5; -.
DR   OMA; PCFAAFP; -.
DR   OrthoDB; 9803297at2; -.
DR   Proteomes; UP000001976; Plasmid pSymA.
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; 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.
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}; Plasmid {ECO:0000313|EMBL:AAK64780.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001976}.
FT   DOMAIN          205..446
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        128
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT   BINDING         92
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         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         212
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         243
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         380
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   SITE            168
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ   SEQUENCE   448 AA;  48904 MW;  1F7C9A9B7B58D5A3 CRC64;
     MNVDEKLEPI LAEVLRRNGG EHEFHQAVRE VLESLGRVIA KHPRYAENAL IERICEPERQ
     IIFRVPWVDD KGQVQINRGF RVQFNSALGP YKGGIRFHPS VNIGIIKFLG FEQTFKNALT
     GMPIGGGKGG SDFNPRGRSD GEIMRFCQSL MTELHRHLGE YTDVPAGDIG VGGREIGYMF
     GQYKRLTNRY EAGVLTGKAL FYGGSRARKE ATGYGATYFV QRMIATKGLD FEGKRVTVSG
     SGNVAIYTME KVIEFGGKIV ACSDSNGYVV DEDGIDLELV KEIKEVRRER ISEYARLKGA
     GTHYIEAGSV WDVPCDVAMP SATQNELTGK DARTLVKNGV LAVGEGANMP CTPEAVRIFQ
     EAGVLFAPGK AANAGGVATS ALEMQQNASR DSWTFEQTEA RLATIMQAIH DRCAETAEEY
     GTPGDYVLGA NIAGFVRVAE AMDALGVI
//
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