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Protein

Phthalate dioxygenase reductase

Gene

ophA1

Organism
Burkholderia cepacia (Pseudomonas cepacia)
Status
Reviewed-Annotation score: Annotation score: 5 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

FMN1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei125FMNCombined sources1 Publication1
Binding sitei226FMNCombined sources1 Publication1
Metal bindingi273Iron-sulfur (2Fe-2S)Combined sources1 Publication1
Binding sitei275FMNCombined sources1 Publication1
Metal bindingi278Iron-sulfur (2Fe-2S)Combined sources1 Publication1
Metal bindingi281Iron-sulfur (2Fe-2S)Combined sources1 Publication1
Metal bindingi309Iron-sulfur (2Fe-2S)Combined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi56 – 57FMNCombined sources1 Publication2
Nucleotide bindingi73 – 75FMNCombined sources1 Publication3
Nucleotide bindingi81 – 84FMNCombined sources1 Publication4

GO - Molecular functioni

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001893982 – 322Phthalate dioxygenase reductaseAdd BLAST321

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1322
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni4 – 8Combined sources5
Beta strandi10 – 21Combined sources12
Beta strandi24 – 30Combined sources7
Beta strandi45 – 49Combined sources5
Beta strandi55 – 59Combined sources5
Beta strandi68 – 75Combined sources8
Helixi83 – 89Combined sources7
Beta strandi96 – 99Combined sources4
Beta strandi113 – 120Combined sources8
Helixi121 – 123Combined sources3
Helixi124 – 137Combined sources14
Beta strandi139 – 149Combined sources11
Helixi151 – 153Combined sources3
Helixi157 – 161Combined sources5
Turni163 – 168Combined sources6
Beta strandi169 – 173Combined sources5
Helixi184 – 188Combined sources5
Beta strandi195 – 201Combined sources7
Helixi203 – 212Combined sources10
Turni213 – 215Combined sources3
Beta strandi221 – 224Combined sources4
Beta strandi239 – 243Combined sources5
Turni244 – 246Combined sources3
Beta strandi249 – 252Combined sources4
Helixi258 – 264Combined sources7
Beta strandi274 – 278Combined sources5
Beta strandi282 – 288Combined sources7
Turni299 – 304Combined sources6
Beta strandi305 – 307Combined sources3
Turni308 – 310Combined sources3
Beta strandi312 – 320Combined sources9

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP33164.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 109FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST103
Domaini239 – 3222Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST84

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

CDDicd00207. fer2. 1 hit.
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.
PIRiA44230.

3D structure databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP33164.

Family and domain databases

CDDicd00207. fer2. 1 hit.
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]
ProtoNetiSearch...

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 2, 2016
This is version 94 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.