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UniProtKB - P33164 (PDR_BURCE)

Entry version 107 (07 Apr 2021)
Sequence version 3 (23 Jan 2007)
Previous versions | rss
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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).

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

FMN1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei125FMNCombined sources1 Publication1
Binding sitei226FMNCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi56 – 57FMNCombined sources1 Publication2
Nucleotide bindingi73 – 75FMNCombined sources1 Publication3
Nucleotide bindingi81 – 84FMNCombined sources1 Publication4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
Biological processElectron transport, Transport
Ligand2Fe-2S, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Phthalate dioxygenase reductase (EC:1.-.-.-)
Short name:
PDR
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ophA1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBurkholderia cepacia (Pseudomonas cepacia)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001893982 – 322Phthalate dioxygenase reductaseAdd BLAST321

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1322
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P33164

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P33164

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini7 – 109FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST103
Domaini239 – 3222Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST84

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the PDR/VanB family.Curated

Family and domain databases

Conserved Domains Database

More...CDDi		cd00207, fer2, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.10.20.30, 1 hit
3.40.50.80, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR036010, 2Fe-2S_ferredoxin-like_sf
IPR001041, 2Fe-2S_ferredoxin-type
IPR006058, 2Fe2S_fd_BS
IPR012675, Beta-grasp_dom_sf
IPR008333, Cbr1-like_FAD-bd_dom
IPR017927, FAD-bd_FR_type
IPR039261, FNR_nucleotide-bd
IPR001433, OxRdtase_FAD/NAD-bd
IPR000951, Ph_dOase_redase
IPR017938, Riboflavin_synthase-like_b-brl

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00970, FAD_binding_6, 1 hit
PF00111, Fer2, 1 hit
PF00175, NAD_binding_1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00409, PHDIOXRDTASE

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52343, SSF52343, 1 hit
SSF54292, SSF54292, 1 hit
SSF63380, SSF63380, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00197, 2FE2S_FER_1, 1 hit
PS51085, 2FE2S_FER_2, 1 hit
PS51384, FAD_FR, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA550988FF80059A6
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AF095748 Genomic DNA Translation: AAD03550.1

Protein sequence database of the Protein Information Resource

More...PIRi		A44230

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2PIAX-ray2.00A2-322[»]
SMRiP33164
ModBaseiSearch...
PDBe-KBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33164

Family and domain databases

CDDicd00207, fer2, 1 hit
Gene3Di3.10.20.30, 1 hit
3.40.50.80, 1 hit
InterProiView protein in InterPro
IPR036010, 2Fe-2S_ferredoxin-like_sf
IPR001041, 2Fe-2S_ferredoxin-type
IPR006058, 2Fe2S_fd_BS
IPR012675, Beta-grasp_dom_sf
IPR008333, Cbr1-like_FAD-bd_dom
IPR017927, FAD-bd_FR_type
IPR039261, FNR_nucleotide-bd
IPR001433, OxRdtase_FAD/NAD-bd
IPR000951, Ph_dOase_redase
IPR017938, Riboflavin_synthase-like_b-brl
PfamiView protein in Pfam
PF00970, FAD_binding_6, 1 hit
PF00111, Fer2, 1 hit
PF00175, NAD_binding_1, 1 hit
PRINTSiPR00409, PHDIOXRDTASE
SUPFAMiSSF52343, SSF52343, 1 hit
SSF54292, SSF54292, 1 hit
SSF63380, SSF63380, 1 hit
PROSITEiView protein in PROSITE
PS00197, 2FE2S_FER_1, 1 hit
PS51085, 2FE2S_FER_2, 1 hit
PS51384, FAD_FR, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPDR_BURCE
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P33164
Secondary accession number(s): Q9ZFR3
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: April 7, 2021
This is version 107 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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
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