ID   MORA_PSEPU              Reviewed;         296 AA.
AC   Q02198;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Morphine 6-dehydrogenase;
DE            EC=1.1.1.218;
DE   AltName: Full=Naloxone reductase;
GN   Name=morA;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OG   Plasmid pMDH7.2.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-26.
RC   STRAIN=M10;
RX   PubMed=8452544; DOI=10.1042/bj2900539;
RA   Willey D.L., Caswell D.A., Lowe C.R., Bruce N.C.;
RT   "Nucleotide sequence and over-expression of morphine dehydrogenase, a
RT   plasmid-encoded gene from Pseudomonas putida M10.";
RL   Biochem. J. 290:539-544(1993).
RN   [2]
RP   SEQUENCE REVISION.
RA   Bruce N.C.;
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 2-26, AND CHARACTERIZATION.
RC   STRAIN=M10;
RX   PubMed=2012614; DOI=10.1042/bj2740875;
RA   Bruce N.C., Wilmot C.J., Jordan K.N., Stephens L.D.G., Lowe C.R.;
RT   "Microbial degradation of the morphine alkaloids. Purification and
RT   characterization of morphine dehydrogenase from Pseudomonas putida M10.";
RL   Biochem. J. 274:875-880(1991).
RN   [4]
RP   SIMILARITY.
RX   PubMed=8192670; DOI=10.1042/bj2990805;
RA   Bruce N.C., Willey D.L., Coulson A.F.W., Jeffery J.;
RT   "Bacterial morphine dehydrogenase further defines a distinct superfamily of
RT   oxidoreductases with diverse functional activities.";
RL   Biochem. J. 299:805-811(1994).
CC   -!- FUNCTION: Oxidizes only the C-6 hydroxy group of morphine and codeine.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=morphine + NAD(+) = H(+) + morphinone + NADH;
CC         Xref=Rhea:RHEA:14317, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57728, ChEBI:CHEBI:57945, ChEBI:CHEBI:58097;
CC         EC=1.1.1.218;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=morphine + NADP(+) = H(+) + morphinone + NADPH;
CC         Xref=Rhea:RHEA:14321, ChEBI:CHEBI:15378, ChEBI:CHEBI:57728,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58097, ChEBI:CHEBI:58349;
CC         EC=1.1.1.218;
CC   -!- PATHWAY: Alkaloid degradation; codeine degradation.
CC   -!- PATHWAY: Alkaloid degradation; morphine degradation.
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR   EMBL; M94775; AAB17356.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q02198; -.
DR   SMR; Q02198; -.
DR   KEGG; ag:AAB17356; -.
DR   UniPathway; UPA00317; -.
DR   UniPathway; UPA00318; -.
DR   GO; GO:0050109; F:morphine 6-dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:2001292; P:codeine catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0071273; P:morphine catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   PANTHER; PTHR43827; PTHR43827; 1.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PIRSF; PIRSF000097; AKR; 1.
DR   PRINTS; PR00069; ALDKETRDTASE.
DR   SUPFAM; SSF51430; SSF51430; 1.
DR   PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR   PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE   1: Evidence at protein level;
KW   Alkaloid metabolism; Direct protein sequencing; NADP; Oxidoreductase;
KW   Plasmid.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2012614,
FT                   ECO:0000269|PubMed:8452544"
FT   CHAIN           2..296
FT                   /note="Morphine 6-dehydrogenase"
FT                   /id="PRO_0000124675"
FT   ACT_SITE        52
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         13..22
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255"
FT   BINDING         110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   296 AA;  32124 MW;  CC16A1DEAE804AA7 CRC64;
     MAGKSPLINL NNGVKMPALG LGVFAASAEE TASAIASAIS SGYRLIDTAR SYNNEAQVGE
     GIRNSGVDRA EMFVTTKLFN CDYGYERALR AFDESLGRLG LDYVDLYLLH WPTKDWNATI
     QSWKAAEKIL GDGRARAIGV CNFLEDQLDE LIAASDVVPA VNQIELHPYF AQKPLLAKNR
     ALGIVTEAWS PIGGAINDGD GDNHGGRKHP LTDPVITTIA EAHGRSAAQV ILRWHFQNDV
     VAIPKSVNPE RIAKNIDVFD FALSDAEMAQ LDELDTGVRI GPDPRDVDTS SFAEFV