ID   DHNO_AGRT7              Reviewed;         413 AA.
AC   P00386;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=D-nopaline dehydrogenase;
DE            EC=1.5.1.19;
DE   AltName: Full=Nopaline synthase;
GN   Name=nos;
OS   Agrobacterium tumefaciens (strain T37).
OG   Plasmid pTiT37.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=176300;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7153689;
RA   Depicker A., Stachel S., Dhaese P., Zambryski P., Goodman H.M.;
RT   "Nopaline synthase: transcript mapping and DNA sequence.";
RL   J. Mol. Appl. Genet. 1:561-573(1982).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6298724; DOI=10.1093/nar/11.2.369;
RA   Bevan M., Barnes W.M., Chilton M.-D.;
RT   "Structure and transcription of the nopaline synthase gene region of T-
RT   DNA.";
RL   Nucleic Acids Res. 11:369-385(1983).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-nopaline + H2O + NADP(+) = 2-oxoglutarate + H(+) + L-
CC         arginine + NADPH; Xref=Rhea:RHEA:19637, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:32682,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58074, ChEBI:CHEBI:58349; EC=1.5.1.19;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the lysopine/nopaline/octopine/opine/vitopine
CC       dehydrogenases family. {ECO:0000305}.
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DR   EMBL; V00087; CAA23427.1; -; Genomic_DNA.
DR   PIR; A92833; DEAGNT.
DR   AlphaFoldDB; P00386; -.
DR   SMR; P00386; -.
DR   BioCyc; MetaCyc:MON-18212; -.
DR   GO; GO:0047829; F:D-nopaline dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR011128; G3P_DH_NAD-dep_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR003421; Opine_DH.
DR   Pfam; PF01210; NAD_Gly3P_dh_N; 1.
DR   Pfam; PF02317; Octopine_DH; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Crown gall tumor; NADP; Oxidoreductase; Plasmid.
FT   CHAIN           1..413
FT                   /note="D-nopaline dehydrogenase"
FT                   /id="PRO_0000179983"
FT   CONFLICT        222
FT                   /note="C -> Y (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        359
FT                   /note="N -> K (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        362
FT                   /note="L -> I (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   413 AA;  45387 MW;  9639D2D73C57CEF8 CRC64;
     MAITLSATSL PISAADHHPL PLTVGVLGSG HAGTALAAWF ASRHVPTALW APADHPGSIS
     AIKANEGVIT TEGMINGPFR VSACDDLAAV IRSSRVLIIV TRADVHDSFV NELANFNGEL
     ATKDIVVVCG HGFSIKYERQ LRFKRIFETD NSPITSKLSD QKKCNVNIKE MKASFGLSCF
     PIHRDDAGVI DLPEDTKNIF AQLFSARIIC IPPLQVLFFS NCITHAVPAV MNIGRLRDPA
     NSLTKRAEKW LLELDERTPR AEKGFFFYGE GSNTYVCNVQ EQIDHERRKV AAACGLRLNS
     LLQECNDEYD TDYETLREYC LAPSPHNVHH ACPDNMEHRY FSEELCSLED VAAIAAIANI
     ELPLTHAFIN IIHAGKGKIN PTGKSSSVIG NFSSSDLIRF GATHVFNKDE MVE