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Reviewed, UniProtKB/Swiss-Prot P00259 (PUTX_PSEPU)

Last modified November 25, 2008. Version 84. 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:
    Putidaredoxin
      Short name=PDX
Gene names
Name: camB
OrganismPseudomonas putida
Taxonomic identifier303 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length107 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Cofactor

Binds 1 2Fe-2S cluster.

Subunit structure

Monomer.

Sequence similarities

Belongs to the adrenodoxin/putidaredoxin family.

Contains 1 2Fe-2S ferredoxin-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 107106Putidaredoxin
PRO_0000201162

Regions

Domain2 – 1061052Fe-2S ferredoxin-type

Sites

Metal binding401Iron-sulfur (2Fe-2S)
Metal binding461Iron-sulfur (2Fe-2S)
Metal binding491Iron-sulfur (2Fe-2S)
Metal binding871Iron-sulfur (2Fe-2S)

Experimental info

Sequence conflict151E → Q AA sequence Ref.3

Secondary structure

..................... 107
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00259-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: F487E481F8BEE2C9

FASTA10711,550
        10         20         30         40         50         60 
MSKVVYVSHD GTRRELDVAD GVSLMQAAVS NGIYDIVGDC GGSASCATCH VYVNEAFTDK 

        70         80         90        100 
VPAANEREIG MLECVTAELK PNSRLCCQII MTPELDGIVV DVPDRQW 

« 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: 2180940] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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: 2613690] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: G1 / ATCC 17453.
[3]"The amino acid sequence of putidaredoxin, an iron-sulfur protein from Pseudomonas putida."
Tanaka M., Haniu M., Yasunobu K.T., Dus K., Gunsalus I.C.
J. Biol. Chem. 249:3689-3701(1974) [PubMed: 4833743] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-107.
[4]"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: 11524002] [Abstract]
Cited for: INTERACTION WITH PUTIDAREDOXIN REDUCTASE.
[5]"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: 15716266] [Abstract]
Cited for: INTERACTION WITH PUTIDAREDOXIN REDUCTASE.
[6]"Crystal structure of putidaredoxin, the [2Fe-2S] component of the P450cam monooxygenase system from Pseudomonas putida."
Sevrioukova I.F., Garcia C., Li H., Bhaskar B., Poulos T.L.
J. Mol. Biol. 333:377-392(2003) [PubMed: 14529624] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) OF MUTANTS.
[7]"Structure of C73G putidaredoxin from Pseudomonas putida."
Smith N., Mayhew M., Holden M.J., Kelly H., Robinson H., Heroux A., Vilker V.L., Gallagher D.T.
Acta Crystallogr. D 60:816-822(2004) [PubMed: 15103126] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT GLY-74.
[8]"Redox-dependent structural reorganization in putidaredoxin, a vertebrate-type [2Fe-2S] ferredoxin from Pseudomonas putida."
Sevrioukova I.F.
J. Mol. Biol. 347:607-621(2005) [PubMed: 15755454] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF MUTANTS SER-74 AND SER-86.
[9]"1H NMR identification of a beta-sheet structure and description of folding topology in putidaredoxin."
Pochapsky T.C., Ye X.M.
Biochemistry 30:3850-3856(1991) [PubMed: 2018758] [Abstract]
Cited for: STRUCTURE BY NMR.
[10]"1H NMR sequential assignments and identification of secondary structural elements in oxidized putidaredoxin, an electron-transfer protein from Pseudomonas."
Ye X.M., Pochapsky T.C., Pochapsky S.S.
Biochemistry 31:1961-1968(1992) [PubMed: 1536837] [Abstract]
Cited for: STRUCTURE BY NMR.
[11]"An NMR-derived model for the solution structure of oxidized putidaredoxin, a 2-Fe, 2-S ferredoxin from Pseudomonas."
Pochapsky T.C., Ye X.M., Ratnaswamy G., Lyons T.A.
Biochemistry 33:6424-6432(1994) [PubMed: 8204575] [Abstract]
Cited for: STRUCTURE BY NMR.
[12]"Redox-dependent 1H NMR spectral features and tertiary structural constraints on the C-terminal region of putidaredoxin."
Pochapsky T.C., Ratnaswamy G., Patera A.
Biochemistry 33:6433-6441(1994) [PubMed: 8204576] [Abstract]
Cited for: STRUCTURE BY NMR.
[13]"The solution structure of a gallium-substituted putidaredoxin mutant: GaPdx C85S."
Pochapsky T.C., Kuti M., Kazanis S.
J. Biomol. NMR 12:407-415(1998) [PubMed: 9835048] [Abstract]
Cited for: STRUCTURE BY NMR.
[14]"A refined model for the solution structure of oxidized putidaredoxin."
Pochapsky T.C., Jain N.U., Kuti M., Lyons T.A., Heymont J.
Biochemistry 38:4681-4690(1999) [PubMed: 10200155] [Abstract]
Cited for: STRUCTURE BY NMR.

Cross-references

Sequence databases

J05406 Genomic DNA. Translation: AAA25759.1.
D00528 Genomic DNA. Translation: BAA00414.1.
PIRPXPSEP. JX0079.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1GPXNMR-A1-107[»]
1OQQX-ray1.47A/B1-107[»]
1OQRX-ray1.65A/B/C1-107[»]
1PDXNMR-A1-107[»]
1PUTNMR-A1-107[»]
1R7SX-ray1.91A/B/C1-107[»]
1XLNX-ray2.03A/B1-107[»]
1XLOX-ray1.84A/B1-107[»]
1XLPX-ray2.00A/B/C1-107[»]
1XLQX-ray1.45A/B/C1-107[»]
1YJINMR-A1-107[»]
1YJJNMR-A1-107[»]
ModBaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MON-3502.

Family and domain databases

InterProIPR001055. Adrenodoxin.
IPR012675. b-grasp_ferredoxin-like.
IPR001041. Ferredoxin.
[Graphical view]
Gene3DG3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
PfamPF00111. Fer2. 1 hit.
[Graphical view]
PRINTSPR00355. ADRENODOXIN.
PROSITEPS51085. 2FE2S_FER_2. 1 hit.
PS00814. ADX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

LinkHubP00259.

Entry information

Entry namePUTX_PSEPU
AccessionPrimary (citable) accession number: P00259
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 25, 2008
This is version 84 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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