Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P33164

- PDR_BURCE

UniProt

P33164 - PDR_BURCE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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 – 103102FMNAdd
BLAST
Nucleotide bindingi113 – 227115NADAdd
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 reductasePRO_0000189398Add
BLAST

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
322
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni4 – 85Combined sources
Beta strandi10 – 2112Combined sources
Beta strandi24 – 307Combined sources
Beta strandi45 – 495Combined sources
Beta strandi55 – 595Combined sources
Beta strandi68 – 758Combined sources
Helixi83 – 897Combined sources
Beta strandi96 – 994Combined sources
Beta strandi113 – 1208Combined sources
Helixi121 – 1233Combined sources
Helixi124 – 13714Combined sources
Beta strandi139 – 14911Combined sources
Helixi151 – 1533Combined sources
Helixi157 – 1615Combined sources
Turni163 – 1686Combined sources
Beta strandi169 – 1735Combined sources
Helixi184 – 1885Combined sources
Beta strandi195 – 2017Combined sources
Helixi203 – 21210Combined sources
Turni213 – 2153Combined sources
Beta strandi221 – 2244Combined sources
Beta strandi239 – 2435Combined sources
Turni244 – 2463Combined sources
Beta strandi249 – 2524Combined sources
Helixi258 – 2647Combined sources
Beta strandi274 – 2785Combined sources
Beta strandi282 – 2887Combined sources
Turni299 – 3046Combined sources
Beta strandi305 – 3073Combined sources
Turni308 – 3103Combined sources
Beta strandi312 – 3209Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PIAX-ray2.00A2-322[»]
ProteinModelPortaliP33164.
SMRiP33164. Positions 2-322.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33164.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Belongs to the PDR/VanB family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation

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

        10         20         30         40         50
MTTPQEDGFL RLKIASKEKI ARDIWSFELT DPQGAPLPPF EAGANLTVAV
60 70 80 90 100
PNGSRRTYSL CNDSQERNRY VIAVKRDSNG RGGSISFIDD TSEGDAVEVS
110 120 130 140 150
LPRNEFPLDK RAKSFILVAG GIGITPMLSM ARQLRAEGLR SFRLYYLTRD
160 170 180 190 200
PEGTAFFDEL TSDEWRSDVK IHHDHGDPTK AFDFWSVFEK SKPAQHVYCC
210 220 230 240 250
GPQALMDTVR DMTGHWPSGT VHFESFGATN TNARENTPFT VRLSRSGTSF
260 270 280 290 300
EIPANRSILE VLRDANVRVP SSCESGTCGS CKTALCSGEA DHRDMVLRDD
310 320
EKGTQIMVCV SRAKSAELVL DL
Length:322
Mass (Da):35,665
Last modified:January 23, 2007 - v3
Checksum:iA550988FF80059A6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF095748 Genomic DNA. Translation: AAD03550.1.
PIRiA44230.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF095748 Genomic DNA. Translation: AAD03550.1 .
PIRi A44230.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 88 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