UniProtKB - P33164 (PDR_BURCE)
Protein
Phthalate dioxygenase reductase
Gene
ophA1
Organism
Burkholderia cepacia (Pseudomonas cepacia)
Status
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 125 | FMNCombined sources1 Publication | 1 | |
Binding sitei | 226 | FMNCombined sources1 Publication | 1 | |
Metal bindingi | 273 | Iron-sulfur (2Fe-2S)Combined sources1 Publication | 1 | |
Binding sitei | 275 | FMNCombined sources1 Publication | 1 | |
Metal bindingi | 278 | Iron-sulfur (2Fe-2S)Combined sources1 Publication | 1 | |
Metal bindingi | 281 | Iron-sulfur (2Fe-2S)Combined sources1 Publication | 1 | |
Metal bindingi | 309 | Iron-sulfur (2Fe-2S)Combined sources1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 56 – 57 | FMNCombined sources1 Publication | 2 | |
Nucleotide bindingi | 73 – 75 | FMNCombined sources1 Publication | 3 | |
Nucleotide bindingi | 81 – 84 | FMNCombined sources1 Publication | 4 |
GO - Molecular functioni
- 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
- electron transfer activity Source: InterPro
- metal ion binding Source: UniProtKB-KW
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Electron transport, Transport |
Ligand | 2Fe-2S, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:ophA1 |
Organismi | Burkholderia cepacia (Pseudomonas cepacia) |
Taxonomic identifieri | 292 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed | |||
ChainiPRO_0000189398 | 2 – 322 | Phthalate dioxygenase reductaseAdd BLAST | 321 |
Interactioni
Subunit structurei
Monomer.
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P33164 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P33164 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 7 – 109 | FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST | 103 | |
Domaini | 239 – 322 | 2Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST | 84 |
Sequence similaritiesi
Belongs to the PDR/VanB family.Curated
Family and domain databases
CDDi | cd00207, fer2, 1 hit |
Gene3Di | 3.10.20.30, 1 hit 3.40.50.80, 1 hit |
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 |
Pfami | View protein in Pfam PF00970, FAD_binding_6, 1 hit PF00111, Fer2, 1 hit PF00175, NAD_binding_1, 1 hit |
PRINTSi | PR00409, PHDIOXRDTASE |
SUPFAMi | SSF52343, SSF52343, 1 hit SSF54292, SSF54292, 1 hit SSF63380, SSF63380, 1 hit |
PROSITEi | View protein in PROSITE PS00197, 2FE2S_FER_1, 1 hit PS51085, 2FE2S_FER_2, 1 hit PS51384, FAD_FR, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P33164-1 [UniParc]FASTAAdd to basket
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF095748 Genomic DNA Translation: AAD03550.1 |
PIRi | A44230 |
Similar proteinsi
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 | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2PIA | X-ray | 2.00 | A | 2-322 | [»] | |
SMRi | P33164 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P33164 |
Family and domain databases
CDDi | cd00207, fer2, 1 hit |
Gene3Di | 3.10.20.30, 1 hit 3.40.50.80, 1 hit |
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 |
Pfami | View protein in Pfam PF00970, FAD_binding_6, 1 hit PF00111, Fer2, 1 hit PF00175, NAD_binding_1, 1 hit |
PRINTSi | PR00409, PHDIOXRDTASE |
SUPFAMi | SSF52343, SSF52343, 1 hit SSF54292, SSF54292, 1 hit SSF63380, SSF63380, 1 hit |
PROSITEi | View protein in PROSITE PS00197, 2FE2S_FER_1, 1 hit PS51085, 2FE2S_FER_2, 1 hit PS51384, FAD_FR, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PDR_BURCE | |
Accessioni | P33164Primary (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: | December 2, 2020 | |
This is version 106 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families