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P33164 (PDR_BURCE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phthalate dioxygenase reductase

Short name=PDR
EC=1.-.-.-
Gene names
Name:ophA1
OrganismBurkholderia cepacia (Pseudomonas cepacia)
Taxonomic identifier292 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length322 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the electron transfer chain involved in pyridine nucleotide-dependent dihydroxylation of phthalate. Utilizes FMN to mediate electron transfer from the two-electron donor, NADH, to the one-electron acceptor, (2Fe-2S).

Cofactor

FMN.

Subunit structure

Monomer.

Sequence similarities

Belongs to the PDR/VanB family.

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

Contains 1 FAD-binding FR-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 322321Phthalate dioxygenase reductase
PRO_0000189398

Regions

Domain7 – 109103FAD-binding FR-type
Domain239 – 322842Fe-2S ferredoxin-type
Nucleotide binding2 – 103102FMN
Nucleotide binding113 – 227115NAD

Sites

Metal binding2731Iron-sulfur (2Fe-2S)
Metal binding2781Iron-sulfur (2Fe-2S)
Metal binding2811Iron-sulfur (2Fe-2S)
Metal binding3091Iron-sulfur (2Fe-2S)

Secondary structure

........................................................ 322
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P33164 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A550988FF80059A6

FASTA32235,665
        10         20         30         40         50         60 
MTTPQEDGFL RLKIASKEKI ARDIWSFELT DPQGAPLPPF EAGANLTVAV PNGSRRTYSL 

        70         80         90        100        110        120 
CNDSQERNRY VIAVKRDSNG RGGSISFIDD TSEGDAVEVS LPRNEFPLDK RAKSFILVAG 

       130        140        150        160        170        180 
GIGITPMLSM ARQLRAEGLR SFRLYYLTRD PEGTAFFDEL TSDEWRSDVK IHHDHGDPTK 

       190        200        210        220        230        240 
AFDFWSVFEK SKPAQHVYCC GPQALMDTVR DMTGHWPSGT VHFESFGATN TNARENTPFT 

       250        260        270        280        290        300 
VRLSRSGTSF EIPANRSILE VLRDANVRVP SSCESGTCGS CKTALCSGEA DHRDMVLRDD 

       310        320 
EKGTQIMVCV SRAKSAELVL DL 

« Hide

References

[1]"Novel organization of the genes for phthalate degradation from Burkholderia cepacia DBO1."
Chang H.K., Zylstra G.J.
J. Bacteriol. 180:6529-6537(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 29424 / DBO1.
[2]"Phthalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotides to [2Fe-2S]."
Correll C.C., Batie C.J., Ballou D.P., Ludwig M.L.
Science 258:1604-1610(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), PARTIAL PROTEIN SEQUENCE.
Strain: ATCC 29424 / DBO1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF095748 Genomic DNA. Translation: AAD03550.1.
PIRA44230.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2PIAX-ray2.00A2-322[»]
ProteinModelPortalP33164.
SMRP33164. Positions 2-322.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.10.20.30. 1 hit.
InterProIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom.
IPR017927. Fd_Rdtase_FAD-bd.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR000951. Ph_dOase_redase.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamPF00970. FAD_binding_6. 1 hit.
PF00111. Fer2. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSPR00409. PHDIOXRDTASE.
SUPFAMSSF54292. SSF54292. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP33164.

Entry information

Entry namePDR_BURCE
AccessionPrimary (citable) accession number: P33164
Secondary accession number(s): Q9ZFR3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 86 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references