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P33164

- PDR_BURCE

UniProt

P33164 - PDR_BURCE

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Protein
Phthalate dioxygenase reductase
Gene
ophA1
Organism
Burkholderia cepacia (Pseudomonas cepacia)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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).

Cofactori

FMN.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi273 – 2731Iron-sulfur (2Fe-2S)
Metal bindingi278 – 2781Iron-sulfur (2Fe-2S)
Metal bindingi281 – 2811Iron-sulfur (2Fe-2S)
Metal bindingi309 – 3091Iron-sulfur (2Fe-2S)

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi2 – 103102FMN
Add
BLAST
Nucleotide bindingi113 – 227115NAD
Add
BLAST

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  2. electron carrier activity Source: InterPro
  3. metal ion binding Source: UniProtKB-KW
  4. oxidoreductase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

2Fe-2S, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Phthalate dioxygenase reductase (EC:1.-.-.-)
Short name:
PDR
Gene namesi
Name:ophA1
OrganismiBurkholderia cepacia (Pseudomonas cepacia)
Taxonomic identifieri292 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 322321Phthalate dioxygenase reductase
PRO_0000189398Add
BLAST

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni4 – 85
Beta strandi10 – 2112
Beta strandi24 – 307
Beta strandi45 – 495
Beta strandi55 – 595
Beta strandi68 – 758
Helixi83 – 897
Beta strandi96 – 994
Beta strandi113 – 1208
Helixi121 – 1233
Helixi124 – 13714
Beta strandi139 – 14911
Helixi151 – 1533
Helixi157 – 1615
Turni163 – 1686
Beta strandi169 – 1735
Helixi184 – 1885
Beta strandi195 – 2017
Helixi203 – 21210
Turni213 – 2153
Beta strandi221 – 2244
Beta strandi239 – 2435
Turni244 – 2463
Beta strandi249 – 2524
Helixi258 – 2647
Beta strandi274 – 2785
Beta strandi282 – 2887
Turni299 – 3046
Beta strandi305 – 3073
Turni308 – 3103
Beta strandi312 – 3209

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PIAX-ray2.00A2-322[»]
ProteinModelPortaliP33164.
SMRiP33164. Positions 2-322.

Miscellaneous databases

EvolutionaryTraceiP33164.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 109103FAD-binding FR-type
Add
BLAST
Domaini239 – 322842Fe-2S ferredoxin-type
Add
BLAST

Sequence similaritiesi

Belongs to the PDR/VanB family.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 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]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00111. Fer2. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00409. PHDIOXRDTASE.
SUPFAMiSSF54292. SSF54292. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P33164-1 [UniParc]FASTAAdd to Basket

« Hide

MTTPQEDGFL RLKIASKEKI ARDIWSFELT DPQGAPLPPF EAGANLTVAV    50
PNGSRRTYSL CNDSQERNRY VIAVKRDSNG RGGSISFIDD TSEGDAVEVS 100
LPRNEFPLDK RAKSFILVAG GIGITPMLSM ARQLRAEGLR SFRLYYLTRD 150
PEGTAFFDEL TSDEWRSDVK IHHDHGDPTK AFDFWSVFEK SKPAQHVYCC 200
GPQALMDTVR DMTGHWPSGT VHFESFGATN TNARENTPFT VRLSRSGTSF 250
EIPANRSILE VLRDANVRVP SSCESGTCGS CKTALCSGEA DHRDMVLRDD 300
EKGTQIMVCV SRAKSAELVL DL 322
Length:322
Mass (Da):35,665
Last modified:January 23, 2007 - v3
Checksum:iA550988FF80059A6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF095748 Genomic DNA. Translation: AAD03550.1.
PIRiA44230.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF095748 Genomic DNA. Translation: AAD03550.1 .
PIRi A44230.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2PIA X-ray 2.00 A 2-322 [» ]
ProteinModelPortali P33164.
SMRi P33164. Positions 2-322.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P33164.

Family and domain databases

Gene3Di 3.10.20.30. 1 hit.
InterProi IPR001041. 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 ]
Pfami PF00970. FAD_binding_6. 1 hit.
PF00111. Fer2. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view ]
PRINTSi PR00409. PHDIOXRDTASE.
SUPFAMi SSF54292. SSF54292. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEi PS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiPDR_BURCE
AccessioniPrimary (citable) accession number: P33164
Secondary accession number(s): Q9ZFR3
Entry historyi
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 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

External Data

Dasty 3

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