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P16640

- CAMA_PSEPU

UniProt

P16640 - CAMA_PSEPU

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Protein
Putidaredoxin reductase
Gene
camA
Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

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 – 3732FAD Reviewed prediction
Add
BLAST
Nucleotide bindingi156 – 16510NAD Reviewed prediction

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
Complete GO annotation...

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 reductase
PRO_0000167646Add
BLAST

Expressioni

Inductioni

By camphor.

Structurei

Secondary structure

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.

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: July 9, 2014
This is version 92 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

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