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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...

GO - Biological processi

    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...

    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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