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P16640

- CAMA_PSEPU

UniProt

P16640 - CAMA_PSEPU

Protein

Putidaredoxin reductase

Gene

camA

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (01 Aug 1990)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Catalytic activityi

    Reduced putidaredoxin + NAD+ = oxidized putidaredoxin + NADH.1 Publication

    Cofactori

    FAD.2 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi6 – 3732FADSequence AnalysisAdd
    BLAST
    Nucleotide bindingi156 – 16510NADSequence Analysis

    GO - Molecular functioni

    1. flavin adenine dinucleotide binding Source: InterPro
    2. oxidoreductase activity Source: UniProtKB-KW

    GO - Biological processi

    1. (+)-camphor catabolic process Source: UniProtKB-UniPathway
    2. cell redox homeostasis Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-3501.
    RETL1328306-WGS:GSTH-1356-MONOMER.
    UniPathwayiUPA00719.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Putidaredoxin reductase (EC:1.18.1.5)
    Alternative name(s):
    Putidaredoxin--NAD+ reductase
    Gene namesi
    Name:camA
    OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
    Taxonomic identifieri303 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 422422Putidaredoxin reductasePRO_0000167646Add
    BLAST

    Expressioni

    Inductioni

    By camphor.

    Structurei

    Secondary structure

    1
    422
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 105
    Helixi14 – 2512
    Beta strandi30 – 356
    Helixi46 – 483
    Turni49 – 557
    Helixi60 – 623
    Beta strandi63 – 653
    Helixi67 – 726
    Beta strandi75 – 784
    Beta strandi83 – 875
    Turni88 – 914
    Beta strandi92 – 954
    Beta strandi100 – 1023
    Beta strandi104 – 1085
    Beta strandi112 – 1143
    Helixi118 – 1203
    Helixi123 – 1264
    Beta strandi130 – 1356
    Helixi136 – 1449
    Beta strandi151 – 1555
    Helixi159 – 17012
    Beta strandi174 – 1785
    Beta strandi180 – 1834
    Turni184 – 1885
    Helixi191 – 20414
    Beta strandi207 – 2093
    Beta strandi214 – 2196
    Turni221 – 2233
    Beta strandi226 – 2316
    Beta strandi236 – 2383
    Beta strandi240 – 2445
    Beta strandi248 – 2503
    Helixi253 – 2575
    Beta strandi262 – 2676
    Beta strandi279 – 2813
    Helixi283 – 2853
    Beta strandi286 – 2905
    Turni291 – 2944
    Beta strandi295 – 2984
    Helixi302 – 31615
    Beta strandi328 – 3336
    Beta strandi336 – 3427
    Beta strandi348 – 3558
    Turni356 – 3594
    Beta strandi360 – 3678
    Beta strandi370 – 3789
    Helixi380 – 39112
    Helixi398 – 4014
    Helixi408 – 42114

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Q1RX-ray1.91A/B1-422[»]
    1Q1WX-ray2.60A/B1-422[»]
    3LB8X-ray2.60A/B2-422[»]
    ProteinModelPortaliP16640.
    SMRiP16640. Positions 2-422.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16640.

    Family & Domainsi

    Family and domain databases

    Gene3Di3.30.390.30. 1 hit.
    InterProiIPR016156. 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.
    IPR028202. Reductase_C.
    [Graphical view]
    PfamiPF00070. Pyr_redox. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    PF14759. Reductase_C. 1 hit.
    [Graphical view]
    PRINTSiPR00368. FADPNR.
    SUPFAMiSSF55424. SSF55424. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P16640-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNANDNVVIV GTGLAGVEVA FGLRASGWEG NIRLVGDATV IPHHLPPLSK    50
    AYLAGKATAE SLYLRTPDAY AAQNIQLLGG TQVTAINRDR QQVILSDGRA 100
    LDYDRLVLAT GGRPRPLPVA SGAVGKANNF RYLRTLEDAE CIRRQLIADN 150
    RLVVIGGGYI GLEVAATAIK ANMHVTLLDT AARVLERVTA PPVSAFYEHL 200
    HREAGVDIRT GTQVCGFEMS TDQQKVTAVL CEDGTRLPAD LVIAGIGLIP 250
    NCELASAAGL QVDNGIVINE HMQTSDPLIM AVGDCARFHS QLYDRWVRIE 300
    SVPNALEQAR KIAAILCGKV PRDEAAPWFW SDQYEIGLKM VGLSEGYDRI 350
    IVRGSLAQPD FSVFYLQGDR VLAVDTVNRP VEFNQSKQII TDRLPVEPNL 400
    LGDESVPLKE IIAAAKAELS SA 422
    Length:422
    Mass (Da):45,579
    Last modified:August 1, 1990 - v1
    Checksum:i704BF52E47491AD1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05406 Genomic DNA. Translation: AAA25758.1.
    D00528 Genomic DNA. Translation: BAA00413.1.
    M12546 Genomic DNA. Translation: AAA25761.1.
    PIRiJX0078.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05406 Genomic DNA. Translation: AAA25758.1 .
    D00528 Genomic DNA. Translation: BAA00413.1 .
    M12546 Genomic DNA. Translation: AAA25761.1 .
    PIRi JX0078.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Q1R X-ray 1.91 A/B 1-422 [» ]
    1Q1W X-ray 2.60 A/B 1-422 [» ]
    3LB8 X-ray 2.60 A/B 2-422 [» ]
    ProteinModelPortali P16640.
    SMRi P16640. Positions 2-422.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00719 .
    BioCyci MetaCyc:MONOMER-3501.
    RETL1328306-WGS:GSTH-1356-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P16640.

    Family and domain databases

    Gene3Di 3.30.390.30. 1 hit.
    InterProi IPR016156. 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.
    IPR028202. Reductase_C.
    [Graphical view ]
    Pfami PF00070. Pyr_redox. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    PF14759. Reductase_C. 1 hit.
    [Graphical view ]
    PRINTSi PR00368. FADPNR.
    SUPFAMi SSF55424. SSF55424. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiCAMA_PSEPU
    AccessioniPrimary (citable) accession number: P16640
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: August 1, 1990
    Last modified: October 1, 2014
    This is version 93 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3