ID   OCDH_MIZYE              Reviewed;         400 AA.
AC   Q8N0P0;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Octopine dehydrogenase {ECO:0000312|EMBL:BAB92087.1};
DE            Short=OcDH {ECO:0000303|PubMed:15565272};
DE            EC=1.5.1.11 {ECO:0000250|UniProtKB:Q9BHM6};
GN   Name=odh {ECO:0000312|EMBL:BAB92087.1};
OS   Mizuhopecten yessoensis (Japanese scallop) (Patinopecten yessoensis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pectinida; Pectinoidea; Pectinidae;
OC   Mizuhopecten.
OX   NCBI_TaxID=6573;
RN   [1] {ECO:0000312|EMBL:BAB92087.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Adductor muscle {ECO:0000269|PubMed:15565272};
RX   PubMed=15565272; DOI=10.1007/s10126-004-2700-6;
RA   Kimura T., Nakano T., Yamaguchi T., Sato M., Ogawa T., Muramoto K.,
RA   Yokoyama T., Kan-No N., Nagahisa E., Janssen F., Grieshaber M.K.;
RT   "Complementary DNA cloning and molecular evolution of opine dehydrogenases
RT   in some marine invertebrates.";
RL   Mar. Biotechnol. 6:493-502(2004).
CC   -!- FUNCTION: Catalyzes the reverse reaction of octopine dehydrogenation.
CC       Acts on L-arginine in preference to other substrates (By similarity).
CC       {ECO:0000250|UniProtKB:Q9BHM6}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-octopine + H2O + NAD(+) = H(+) + L-arginine + NADH +
CC         pyruvate; Xref=Rhea:RHEA:16285, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:32682, ChEBI:CHEBI:57520,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.5.1.11;
CC         Evidence={ECO:0000250|UniProtKB:Q9BHM6};
CC   -!- SIMILARITY: Belongs to the lysopine/nopaline/octopine/opine/vitopine
CC       dehydrogenases family. {ECO:0000255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB085183; BAB92087.1; -; mRNA.
DR   AlphaFoldDB; Q8N0P0; -.
DR   SMR; Q8N0P0; -.
DR   GO; GO:0047830; F:D-octopine dehydrogenase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR003421; Opine_DH.
DR   Pfam; PF02317; Octopine_DH; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..400
FT                   /note="Octopine dehydrogenase"
FT                   /id="PRO_0000414625"
FT   ACT_SITE        212
FT                   /evidence="ECO:0000250|UniProtKB:Q9BHM6"
FT   BINDING         10..13
FT                   /ligand="NADH"
FT                   /ligand_id="ChEBI:CHEBI:57945"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BHM6"
FT   BINDING         35..38
FT                   /ligand="NADH"
FT                   /ligand_id="ChEBI:CHEBI:57945"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BHM6"
FT   BINDING         118
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BHM6"
FT   BINDING         118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BHM6"
FT   BINDING         148
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BHM6"
FT   BINDING         212
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BHM6"
FT   BINDING         324
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   400 AA;  43417 MW;  49DA6D05DA6B6791 CRC64;
     MTLKVCVCGG GNGAHTLSGL AASRDGVEVR VLTLFADEAE RWTKALGADE LTVIVNEKDG
     TQTEVKSRPK VITKDPQVAI TGADVVILTV PAFAHEGYFQ AMAPYVQDSA LIVGLPSQAG
     FEFQCRDILG DKAAAVSMMS FETLPWACRI KEFGRKVEVL GTKSVLAASL IKGTAETVDP
     LSTLQKLHGA EPVFRLAKHF LEMLIMSYSF VHPAILYGRW GSWDGNPVSE APLFYQGIDQ
     ATADMLTACS DECKAVGNAI MAACPGNDLS DVKDIYQWYL EYYHEDIQDD HDLYHAITTN
     KSYKGLVHPV KTVDGGVAPD FGNRYLTEDI PMGMIVFKGV AIAAGVPIPN NDKLITWAQE
     KIGKVYLVDG ALTGKDVATT RCPQRYGFNT LNAILTGKKE