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Protein

Putidaredoxin

Gene

camB

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed-Annotation score: Annotation score: 4 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.

Cofactori

[2Fe-2S] clusterNote: Binds 1 [2Fe-2S] cluster.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi40 – 401Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1 Publication
Metal bindingi46 – 461Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1 Publication
Metal bindingi49 – 491Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1 Publication
Metal bindingi87 – 871Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3502.

Names & Taxonomyi

Protein namesi
Recommended name:
Putidaredoxin
Short name:
PDX
Gene namesi
Name:camB
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 107106PutidaredoxinPRO_0000201162Add
BLAST

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

DIPiDIP-29810N.

Structurei

Secondary structure

1
107
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75Combined sources
Helixi9 – 113Combined sources
Beta strandi13 – 175Combined sources
Beta strandi20 – 234Combined sources
Helixi24 – 307Combined sources
Helixi34 – 363Combined sources
Beta strandi38 – 403Combined sources
Beta strandi42 – 465Combined sources
Beta strandi50 – 534Combined sources
Turni55 – 573Combined sources
Helixi58 – 603Combined sources
Helixi66 – 727Combined sources
Beta strandi74 – 774Combined sources
Beta strandi83 – 853Combined sources
Helixi86 – 883Combined sources
Helixi93 – 953Combined sources
Beta strandi98 – 1014Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GPXNMR-A2-107[»]
1OQQX-ray1.47A/B2-107[»]
1OQRX-ray1.65A/B/C2-107[»]
1PDXNMR-A2-107[»]
1PUTNMR-A2-107[»]
1R7SX-ray1.91A/B/C2-107[»]
1XLNX-ray2.03A/B2-107[»]
1XLOX-ray1.84A/B2-107[»]
1XLPX-ray2.00A/B/C2-107[»]
1XLQX-ray1.45A/B/C2-107[»]
1YJINMR-A2-107[»]
1YJJNMR-A2-107[»]
2M56NMR-B2-107[»]
3LB8X-ray2.60C/D2-107[»]
3W9CX-ray2.50B2-107[»]
4JWSX-ray2.15C/D2-107[»]
4JWUX-ray2.20C/D1-107[»]
4JX1X-ray2.09C/D/G/H1-107[»]
ProteinModelPortaliP00259.
SMRiP00259. Positions 2-107.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00259.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 1061052Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the adrenodoxin/putidaredoxin family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR001055. Adrenodoxin.
IPR018298. Adrenodoxin_Fe-S_BS.
IPR012675. Beta-grasp_dom.
[Graphical view]
PfamiPF00111. Fer2. 1 hit.
[Graphical view]
PRINTSiPR00355. ADRENODOXIN.
SUPFAMiSSF54292. SSF54292. 1 hit.
PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
PS00814. ADX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00259-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKVVYVSHD GTRRELDVAD GVSLMQAAVS NGIYDIVGDC GGSASCATCH
60 70 80 90 100
VYVNEAFTDK VPAANEREIG MLECVTAELK PNSRLCCQII MTPELDGIVV

DVPDRQW
Length:107
Mass (Da):11,550
Last modified:January 23, 2007 - v3
Checksum:iF487E481F8BEE2C9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151E → Q AA sequence (PubMed:4833743).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05406 Genomic DNA. Translation: AAA25759.1.
D00528 Genomic DNA. Translation: BAA00414.1.
PIRiJX0079. PXPSEP.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05406 Genomic DNA. Translation: AAA25759.1.
D00528 Genomic DNA. Translation: BAA00414.1.
PIRiJX0079. PXPSEP.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GPXNMR-A2-107[»]
1OQQX-ray1.47A/B2-107[»]
1OQRX-ray1.65A/B/C2-107[»]
1PDXNMR-A2-107[»]
1PUTNMR-A2-107[»]
1R7SX-ray1.91A/B/C2-107[»]
1XLNX-ray2.03A/B2-107[»]
1XLOX-ray1.84A/B2-107[»]
1XLPX-ray2.00A/B/C2-107[»]
1XLQX-ray1.45A/B/C2-107[»]
1YJINMR-A2-107[»]
1YJJNMR-A2-107[»]
2M56NMR-B2-107[»]
3LB8X-ray2.60C/D2-107[»]
3W9CX-ray2.50B2-107[»]
4JWSX-ray2.15C/D2-107[»]
4JWUX-ray2.20C/D1-107[»]
4JX1X-ray2.09C/D/G/H1-107[»]
ProteinModelPortaliP00259.
SMRiP00259. Positions 2-107.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29810N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3502.

Miscellaneous databases

EvolutionaryTraceiP00259.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR001055. Adrenodoxin.
IPR018298. Adrenodoxin_Fe-S_BS.
IPR012675. Beta-grasp_dom.
[Graphical view]
PfamiPF00111. Fer2. 1 hit.
[Graphical view]
PRINTSiPR00355. ADRENODOXIN.
SUPFAMiSSF54292. SSF54292. 1 hit.
PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
PS00814. ADX. 1 hit.
[Graphical view]
ProtoNetiSearch...

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].
  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. "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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) OF MUTANTS.
  7. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiPUTX_PSEPU
AccessioniPrimary (citable) accession number: P00259
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.