Reviewed, UniProtKB/Swiss-Prot Q51697 (IORA_BREDI)

Names and origin

Protein names

Recommended name:
    Isoquinoline 1-oxidoreductase subunit alpha
    EC=1.3.99.16

Gene names

Name:

iorA

Organism

Brevundimonas diminuta (Pseudomonas diminuta)

Taxonomic identifier

293 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Caulobacterales › Caulobacteraceae › Brevundimonas

Protein attributes

Sequence length	152 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.

Ontologies

Keywords
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW isoquinoline 1-oxidoreductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 152	152	Isoquinoline 1-oxidoreductase subunit alpha		PRO_0000189410
Regions
	Domain	1 – 77	77	2Fe-2S ferredoxin-type
Sites
	Metal binding	39	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	44	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	47	1	Iron-sulfur (2Fe-2S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q51697-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 080CD595A6943FFC	FASTA	152	16,410
	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

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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z48918 Genomic DNA. Translation: CAA88753.1.
PIR	A56939.
3D structure databases
HSSP	HSSP built from PDB template 1DGJ based on UniProtKB Q9REC4.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.3.99.16. 259958.
Family and domain databases
InterPro	IPR002888. 2Fe-2S_bd. IPR006058. 2Fe2S_fd_BS. IPR001041. Ferredoxin. [Graphical view]
Pfam	PF00111. Fer2. 1 hit. PF01799. Fer2_2. 1 hit. [Graphical view]
ProDom	PD186071. 2Fe-2S_bind. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

IORA_BREDI

Accession

Primary (citable) accession number: Q51697

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	January 20, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)