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P16640 (CAMA_PSEPU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Putidaredoxin reductase
EC=1.18.1.5
Alternative name(s):
Putidaredoxin--NAD+ reductase
Gene names
Name:camA
OrganismPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifier303 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas ›

Protein attributes

Sequence length422 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The oxidation of camphor by cytochrome P450-CAM requires the participation of a flavoprotein, putidaredoxin reductase, and an iron-sulfur protein, putidaredoxin, to mediate the transfer of electrons from NADH to P450 for oxygen activation. Ref.4

Catalytic activity

Reduced putidaredoxin + NAD+ = oxidized putidaredoxin + NADH. Ref.4

Cofactor

FAD. Ref.4 Ref.7

Pathway

Terpene metabolism; (R)-camphor degradation.

Induction

By camphor.

Ontologies

Keywords
   LigandFAD
Flavoprotein
NAD
   Molecular functionOxidoreductase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_process(+)-camphor catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

cell redox homeostasis

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: InterPro

   Molecular_functionflavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

oxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 422422Putidaredoxin reductase
PRO_0000167646

Regions

Nucleotide binding6 – 3732FAD Potential
Nucleotide binding156 – 16510NAD Potential

Secondary structure

1 ........................................................................................ 422
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16640 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 704BF52E47491AD1

FASTA42245,579
        10         20         30         40         50         60 
MNANDNVVIV GTGLAGVEVA FGLRASGWEG NIRLVGDATV IPHHLPPLSK AYLAGKATAE 

        70         80         90        100        110        120 
SLYLRTPDAY AAQNIQLLGG TQVTAINRDR QQVILSDGRA LDYDRLVLAT GGRPRPLPVA 

       130        140        150        160        170        180 
SGAVGKANNF RYLRTLEDAE CIRRQLIADN RLVVIGGGYI GLEVAATAIK ANMHVTLLDT 

       190        200        210        220        230        240 
AARVLERVTA PPVSAFYEHL HREAGVDIRT GTQVCGFEMS TDQQKVTAVL CEDGTRLPAD 

       250        260        270        280        290        300 
LVIAGIGLIP NCELASAAGL QVDNGIVINE HMQTSDPLIM AVGDCARFHS QLYDRWVRIE 

       310        320        330        340        350        360 
SVPNALEQAR KIAAILCGKV PRDEAAPWFW SDQYEIGLKM VGLSEGYDRI IVRGSLAQPD 

       370        380        390        400        410        420 
FSVFYLQGDR VLAVDTVNRP VEFNQSKQII TDRLPVEPNL LGDESVPLKE IIAAAKAELS 


SA

« Hide

References

[1]"Putidaredoxin reductase and putidaredoxin. Cloning, sequence determination, and heterologous expression of the proteins."
Peterson J.A., Lorence M.C., Amarneh B.
J. Biol. Chem. 265:6066-6073(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: G1 / ATCC 17453.
[2]"Cloning and nucleotide sequences of NADH-putidaredoxin reductase gene (camA) and putidaredoxin gene (camB) involved in cytochrome P-450cam hydroxylase of Pseudomonas putida."
Koga H., Yamaguchi E., Matsunaga K., Aramaki H., Horiuchi T.
J. Biochem. 106:831-836(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: G1 / ATCC 17453.
[3]"Nucleotide sequence of the Pseudomonas putida cytochrome P-450cam gene and its expression in Escherichia coli."
Unger B.P., Gunsalus I.C., Sligar S.G.
J. Biol. Chem. 261:1158-1163(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-51.
[4]"Putidaredoxin reductase, a new function for an old protein."
Sevrioukova I.F., Poulos T.L.
J. Biol. Chem. 277:25831-25839(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, COFACTOR, FUNCTION.
[5]"Laser flash induced electron transfer in P450cam monooxygenase: putidaredoxin reductase-putidaredoxin interaction."
Sevrioukova I.F., Hazzard J.T., Tollin G., Poulos T.L.
Biochemistry 40:10592-10600(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PUTIDAREDOXIN.
[6]"The putidaredoxin reductase-putidaredoxin electron transfer complex: theoretical and experimental studies."
Kuznetsov V.Y., Blair E., Farmer P.J., Poulos T.L., Pifferitti A., Sevrioukova I.F.
J. Biol. Chem. 280:16135-16142(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PUTIDAREDOXIN.
[7]"Crystal structure of putidaredoxin reductase from Pseudomonas putida, the final structural component of the cytochrome P450cam monooxygenase."
Sevrioukova I.F., Li H., Poulos T.L.
J. Mol. Biol. 336:889-902(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH FAD, COFACTOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J05406 Genomic DNA. Translation: AAA25758.1.
D00528 Genomic DNA. Translation: BAA00413.1.
M12546 Genomic DNA. Translation: AAA25761.1.
PIRJX0078.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q1RX-ray1.91A/B1-422[»]
1Q1WX-ray2.60A/B1-422[»]
3LB8X-ray2.60A/B2-422[»]
ProteinModelPortalP16640.
SMRP16640. Positions 2-422.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-3501.
UniPathwayUPA00719.

Family and domain databases

Gene3D3.30.390.30. 1 hit.
InterProIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP16640.

Entry information

Entry nameCAMA_PSEPU
AccessionPrimary (citable) accession number: P16640
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: April 3, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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