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Q51697 (IORA_BREDI) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Isoquinoline 1-oxidoreductase subunit alpha

EC=1.3.99.16
Gene names
Name:iorA
OrganismBrevundimonas diminuta (Pseudomonas diminuta)
Taxonomic identifier293 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeBrevundimonas

Protein attributes

Sequence length152 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Specific towards N-containing N-heterocyclic substrates, including isoquinoline, isoquinolin-5-ol, phthalazine and quinazoline.

Catalytic activity

Isoquinoline + acceptor + H2O = isoquinolin-1(2H)-one + reduced acceptor.

Subunit structure

Heterodimer of an alpha chain and a beta chain.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 152152Isoquinoline 1-oxidoreductase subunit alpha
PRO_0000189410

Regions

Domain1 – 77772Fe-2S ferredoxin-type

Sites

Metal binding391Iron-sulfur (2Fe-2S) By similarity
Metal binding441Iron-sulfur (2Fe-2S) By similarity
Metal binding471Iron-sulfur (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q51697 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 080CD595A6943FFC

FASTA15216,410
        10         20         30         40         50         60 
MIEFILNGQP VRVTEVPEDA PLLWVVREHL KLSGTKFGCG LGLCGACTVH INGEAARSCI 

        70         80         90        100        110        120 
TPLSVVARQS VTTIEGLDPQ HAHPLQRAWI AEQVPQCGYC QSGQIMQAAA LLKKVPKPSD 

       130        140        150 
AQIVEAMDGN LCRCGTYQRI KIAIHRAAKE AA 

« Hide

References

[1]"Molecular cloning of the isoquinoline 1-oxidoreductase genes from Pseudomonas diminuta 7, structural analysis of iorA and iorB, and sequence comparisons with other molybdenum-containing hydroxylases."
Lehmann M., Tshisuaka B., Fetzner S., Lingens F.Y.
J. Biol. Chem. 270:14420-14429(1995) [PubMed: 7782304] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 7.
[2]"Purification and characterization of isoquinoline 1-oxidoreductase from Pseudomonas diminuta 7, a novel molybdenum-containing hydroxylase."
Lehmann M., Tshisuaka B., Fetzner S., Roger P., Lingens F.Y.
J. Biol. Chem. 269:11254-11260(1994) [PubMed: 8157655] [Abstract]
Cited for: CHARACTERIZATION.
Strain: 7.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z48918 Genomic DNA. Translation: CAA88753.1.
PIRA56939.

3D structure databases

ProteinModelPortalQ51697.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA1.3.99.16. 982.

Family and domain databases

InterProIPR002888. 2Fe-2S-bd.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_ferredoxin-type.
IPR001041. Ferredoxin.
[Graphical view]
Gene3DG3DSA:1.10.150.120. 2Fe-2S-bd. 1 hit.
G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
PfamPF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
SUPFAMSSF47741. 2Fe-2S_bind. 1 hit.
SSF54292. Ferredoxin. 1 hit.
PROSITEPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIORA_BREDI
AccessionPrimary (citable) accession number: Q51697
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: September 21, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families