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Reviewed, UniProtKB/Swiss-Prot Q02198 (MORA_PSEPU)

Last modified June 16, 2009. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Morphine 6-dehydrogenase
    EC=1.1.1.218
Alternative name(s):
    Naloxone reductase
Gene names
Name: morA
Encoded onPlasmid pMDH7.2
OrganismPseudomonas putida
Taxonomic identifier303 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length296 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Oxidizes only the C-6 hydroxy group of morphine and codeine.

Catalytic activity

Morphine + NAD(P)+ = morphinone + NAD(P)H.

Pathway

Alkaloid degradation; codeine degradation.

Alkaloid degradation; morphine degradation.

Subunit structure

Monomer.

Sequence similarities

Belongs to the aldo/keto reductase family.

Ontologies

Keywords
   Biological processAlkaloid metabolism
   LigandNADP
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Plasmid
Gene Ontology (GO)
   Biological processalkaloid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionmorphine 6-dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1 Ref.3
Chain2 – 296295Morphine 6-dehydrogenase
PRO_0000124675

Regions

Nucleotide binding13 – 2210NADP Potential

Sites

Active site521Proton donor By similarity
Binding site1101Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q02198-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: CC16A1DEAE804AA7

FASTA29632,124
        10         20         30         40         50         60 
MAGKSPLINL NNGVKMPALG LGVFAASAEE TASAIASAIS SGYRLIDTAR SYNNEAQVGE 

        70         80         90        100        110        120 
GIRNSGVDRA EMFVTTKLFN CDYGYERALR AFDESLGRLG LDYVDLYLLH WPTKDWNATI 

       130        140        150        160        170        180 
QSWKAAEKIL GDGRARAIGV CNFLEDQLDE LIAASDVVPA VNQIELHPYF AQKPLLAKNR 

       190        200        210        220        230        240 
ALGIVTEAWS PIGGAINDGD GDNHGGRKHP LTDPVITTIA EAHGRSAAQV ILRWHFQNDV 

       250        260        270        280        290 
VAIPKSVNPE RIAKNIDVFD FALSDAEMAQ LDELDTGVRI GPDPRDVDTS SFAEFV 

« Hide

References

[1]"Nucleotide sequence and over-expression of morphine dehydrogenase, a plasmid-encoded gene from Pseudomonas putida M10."
Willey D.L., Caswell D.A., Lowe C.R., Bruce N.C.
Biochem. J. 290:539-544(1993) [PubMed: 8452544] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-26.
Strain: M10.
[2]Bruce N.C.
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Microbial degradation of the morphine alkaloids. Purification and characterization of morphine dehydrogenase from Pseudomonas putida M10."
Bruce N.C., Wilmot C.J., Jordan K.N., Stephens L.D.G., Lowe C.R.
Biochem. J. 274:875-880(1991) [PubMed: 2012614] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-26, CHARACTERIZATION.
Strain: M10.
[4]"Bacterial morphine dehydrogenase further defines a distinct superfamily of oxidoreductases with diverse functional activities."
Bruce N.C., Willey D.L., Coulson A.F.W., Jeffery J.
Biochem. J. 299:805-811(1994) [PubMed: 8192670] [Abstract]
Cited for: SIMILARITY.

Cross-references

Sequence databases

M94775 Genomic DNA. Translation: AAB17356.1.

3D structure databases

HSSPHSSP built from PDB template 1HW6 based on UniProtKB P06632.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.1.1.218. 403.

Family and domain databases

InterProIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
[Graphical view]
Gene3DG3DSA:3.20.20.100. Aldo/ket_red. 1 hit.
PANTHERPTHR11732. Aldo/ket_red. 1 hit.
PfamPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
ProDomPD000288. Aldo/ket_red. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. False negative.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMORA_PSEPU
AccessionPrimary (citable) accession number: Q02198
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 56 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents