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Database: UniProt
Entry: A0A397ZXF7_BRACM
LinkDB: A0A397ZXF7_BRACM
Original site: A0A397ZXF7_BRACM 
ID   A0A397ZXF7_BRACM        Unreviewed;       411 AA.
AC   A0A397ZXF7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN   ORFNames=BRAA03T09678Z {ECO:0000313|EMBL:VDC78460.1},
GN   BRAPAZ1V2_A03P03210.2 {ECO:0000313|EMBL:CAG7878978.1}, BRARA_C00293
GN   {ECO:0000313|EMBL:RID68110.1};
OS   Brassica campestris (Field mustard).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3711 {ECO:0000313|EMBL:RID68110.1, ECO:0000313|Proteomes:UP000264353};
RN   [1] {ECO:0000313|EMBL:RID68110.1, ECO:0000313|Proteomes:UP000264353}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. B-3 {ECO:0000313|Proteomes:UP000264353};
RA   Bowman J., Kohchi T., Yamato K., Jenkins J., Shu S., Ishizaki K.,
RA   Yamaoka S., Nishihama R., Nakamura Y., Berger F., Adam C., Aki S.,
RA   Althoff F., Araki T., Arteaga-Vazquez M., Balasubrmanian S., Bauer D.,
RA   Boehm C., Briginshaw L., Caballero-Perez J., Catarino B., Chen F.,
RA   Chiyoda S., Chovatia M., Davies K., Delmans M., Demura T., Dierschke T.,
RA   Dolan L., Dorantes-Acosta A., Eklund D., Florent S., Flores-Sandoval E.,
RA   Fujiyama A., Fukuzawa H., Galik B., Grimanelli D., Grimwood J.,
RA   Grossniklaus U., Hamada T., Haseloff J., Hetherington A., Higo A.,
RA   Hirakawa Y., Hundley H., Ikeda Y., Inoue K., Inoue S., Ishida S., Jia Q.,
RA   Kakita M., Kanazawa T., Kawai Y., Kawashima T., Kennedy M., Kinose K.,
RA   Kinoshita T., Kohara Y., Koide E., Komatsu K., Kopischke S., Kubo M.,
RA   Kyozuka J., Lagercrantz U., Lin S., Lindquist E., Lipzen A., Lu C.,
RA   Luna E., Martienssen R., Minamino N., Mizutani M., Mizutani M.,
RA   Mochizuki N., Monte I., Mosher R., Nagasaki H., Nakagami H., Naramoto S.,
RA   Nishitani K., Ohtani M., Okamoto T., Okumura M., Phillips J., Pollak B.,
RA   Reinders A., Roevekamp M., Sano R., Sawa S., Schmid M., Shirakawa M.,
RA   Solano R., Spunde A., Suetsugu N., Sugano S., Sugiyama A., Sun R.,
RA   Suzuki Y., Takenaka M., Takezawa D., Tomogane H., Tsuzuki M., Ueda T.,
RA   Umeda M., Ward J., Watanabe Y., Yazaki K., Yokoyama R., Yoshitake Y.,
RA   Yotsui I., Zachgo S., Schmutz J.;
RT   "WGS assembly of Brassica rapa FPsc.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAG7878978.1, ECO:0000313|Proteomes:UP000694005}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Genoscope - CEA;
RA   William W.;
RL   Submitted (JUL-2021) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH +
CC         NH4(+); Xref=Rhea:RHEA:15133, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00023525};
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=1.4.1.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00023549};
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; LS974619; CAG7878978.1; -; Genomic_DNA.
DR   EMBL; CM010630; RID68110.1; -; Genomic_DNA.
DR   EMBL; LR031572; VDC78460.1; -; Genomic_DNA.
DR   RefSeq; XP_009130990.1; XM_009132742.2.
DR   GeneID; 103855726; -.
DR   KEGG; brp:103855726; -.
DR   OrthoDB; 45283at2759; -.
DR   Proteomes; UP000264353; Chromosome a3.
DR   Proteomes; UP000694005; Chromosome A03.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:InterPro.
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:SF24; GLUTAMATE DEHYDROGENASE 2; 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          178..408
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        102
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT   BINDING         66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         185
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         216
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         344
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   SITE            142
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ   SEQUENCE   411 AA;  44678 MW;  00581692F51B4B3D CRC64;
     MNALAATNRN FRHASRILGL DSKIEKSLMI PFREIKVECT IPKDDGTLVS YIGFRVQHDN
     SRGPMKGGIR YHPEVDPDEV NALAQLMTWK TAVADIPYGG AKGGIGCSPR DLSLSELERL
     TRVFTQKIHD LIGIHTDVPA PDMGTNAQTM AWILDEYSKF HGHSPAVVTG KPIDLGGSLG
     REAATGRGVV YATEALLAEY GKSIQGLTFV VQGFGNVGTW AAKLIHEKGG KVVAVSDITG
     AVRNPEGIDI NALLKHKEAT GSLNEFTGGD AMDSDELLLH ECDVLIPCAL GGVLNKENAA
     DVKAKFIVEA ANHPTDPDAD EILSKKGVII LPDIYANAGG VTVSYFEWVQ NIQGFMWEEE
     KVNLELQKYM TRAFHNIKTM CHTHSCNLRM GAFTLGVSRV ARATQLRGWE A
//
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