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Protein
Submitted name:

Quinoline 2-oxidoreductase

Gene

qorS

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi48 – 481Iron-sulfur (2Fe-2S) 1Combined sources
Metal bindingi49 – 491Iron-sulfur (2Fe-2S) 1; via amide nitrogenCombined sources
Metal bindingi51 – 511Iron-sulfur (2Fe-2S) 1Combined sources
Metal bindingi53 – 531Iron-sulfur (2Fe-2S) 1Combined sources
Metal bindingi56 – 561Iron-sulfur (2Fe-2S) 1Combined sources
Metal bindingi68 – 681Iron-sulfur (2Fe-2S) 1Combined sources
Metal bindingi107 – 1071Iron-sulfur (2Fe-2S) 2Combined sources
Metal bindingi110 – 1101Iron-sulfur (2Fe-2S) 2Combined sources
Metal bindingi142 – 1421Iron-sulfur (2Fe-2S) 2Combined sources
Metal bindingi144 – 1441Iron-sulfur (2Fe-2S) 2Combined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

2Fe-2SUniRule annotationCombined sources, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BRENDAi1.3.99.17. 5092.

Names & Taxonomyi

Protein namesi
Submitted name:
Quinoline 2-oxidoreductaseImported
Submitted name:
Quinoline 2-oxidoreductase small subunitImported
Gene namesi
Name:qorSImported
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)Imported
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T3QX-ray1.80A/D1-168[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 86772Fe-2S ferredoxin-typeInterPro annotationAdd
BLAST

Sequence similaritiesi

Contains 1 2Fe-2S ferredoxin-type domain.UniRule annotation

Family and domain databases

Gene3Di1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
InterProiIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom.
[Graphical view]
PfamiPF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
SUPFAMiSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P72223-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQAHEESQLM RISATINGKP RVFYVEPRMH LADALREVVG LTGTKIGCEQ
60 70 80 90 100
GVCGSCTILI DGAPMRSCLT LAVQAEGCSI ETVEGLSQGE KLNALQDSFR
110 120 130 140 150
RHHALQCGFC TAGMLATARS ILAENPAPSR DEVREVMSGN LCRCTGYETI
160
IDAITDPAVA EAARRGEV
Length:168
Mass (Da):18,024
Last modified:February 1, 1997 - v1
Checksum:i246E5216DCC1BC72
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98131 Genomic DNA. Translation: CAA66829.1.
AJ583091 Genomic DNA. Translation: CAE47364.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98131 Genomic DNA. Translation: CAA66829.1.
AJ583091 Genomic DNA. Translation: CAE47364.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T3QX-ray1.80A/D1-168[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.3.99.17. 5092.

Family and domain databases

Gene3Di1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
InterProiIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom.
[Graphical view]
PfamiPF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
SUPFAMiSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning, expression and sequence analysis of the Three genes encoding Quinoline 2-Oxidoreductase, a molybdenum-containing hydroxylase from Pseudomonas putida 86*."
    Blaese M.A., Bruntner C., Tshisuaka B., Fetzner S., Lingens F.
    J. Biol. Chem. 271:23068-23079(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 86Imported.
  2. "Sequence and transcriptional analysis of a gene cluster of Pseudomonas putida 86 involved in quinoline degradation."
    Carl B., Arnold A., Hauer B., Fetzner S.
    Gene 331:177-188(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  3. "Active site geometry and substrate recognition of the molybdenum hydroxylase quinoline 2-oxidoreductase."
    Bonin I., Martins B.M., Purvanov V., Fetzner S., Huber R., Dobbek H.
    Structure 12:1425-1435(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (2FE-2S).

Entry informationi

Entry nameiP72223_PSEPU
AccessioniPrimary (citable) accession number: P72223
Entry historyi
Integrated into UniProtKB/TrEMBL: February 1, 1997
Last sequence update: February 1, 1997
Last modified: July 6, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.