IORA_BREDI
ID IORA_BREDI Reviewed; 152 AA.
AC Q51697;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Isoquinoline 1-oxidoreductase subunit alpha;
DE EC=1.3.99.16;
GN Name=iorA;
OS Brevundimonas diminuta (Pseudomonas diminuta).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=293;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=7;
RX PubMed=7782304; DOI=10.1074/jbc.270.24.14420;
RA Lehmann M., Tshisuaka B., Fetzner S., Lingens F.Y.;
RT "Molecular cloning of the isoquinoline 1-oxidoreductase genes from
RT Pseudomonas diminuta 7, structural analysis of iorA and iorB, and sequence
RT comparisons with other molybdenum-containing hydroxylases.";
RL J. Biol. Chem. 270:14420-14429(1995).
RN [2]
RP CHARACTERIZATION.
RC STRAIN=7;
RX PubMed=8157655; DOI=10.1016/s0021-9258(19)78118-6;
RA Lehmann M., Tshisuaka B., Fetzner S., Roger P., Lingens F.Y.;
RT "Purification and characterization of isoquinoline 1-oxidoreductase from
RT Pseudomonas diminuta 7, a novel molybdenum-containing hydroxylase.";
RL J. Biol. Chem. 269:11254-11260(1994).
CC -!- FUNCTION: Specific towards N-containing N-heterocyclic substrates,
CC including isoquinoline, isoquinolin-5-ol, phthalazine and quinazoline.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + H2O + isoquinoline = AH2 + isoquinolin-1(2H)-one;
CC Xref=Rhea:RHEA:11588, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16092, ChEBI:CHEBI:17499, ChEBI:CHEBI:18350;
CC EC=1.3.99.16;
CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain.
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DR EMBL; Z48918; CAA88753.1; -; Genomic_DNA.
DR PIR; A56939; A56939.
DR AlphaFoldDB; Q51697; -.
DR SMR; Q51697; -.
DR KEGG; ag:CAA88753; -.
DR BioCyc; MetaCyc:MON-20838; -.
DR BRENDA; 1.3.99.16; 982.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0047121; F:isoquinoline 1-oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR002888; 2Fe-2S-bd.
DR InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF01799; Fer2_2; 1.
DR SUPFAM; SSF47741; SSF47741; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Iron; Iron-sulfur; Metal-binding; Oxidoreductase.
FT CHAIN 1..152
FT /note="Isoquinoline 1-oxidoreductase subunit alpha"
FT /id="PRO_0000189410"
FT DOMAIN 1..77
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 39
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 44
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 47
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 152 AA; 16410 MW; 080CD595A6943FFC CRC64;
MIEFILNGQP VRVTEVPEDA PLLWVVREHL KLSGTKFGCG LGLCGACTVH INGEAARSCI
TPLSVVARQS VTTIEGLDPQ HAHPLQRAWI AEQVPQCGYC QSGQIMQAAA LLKKVPKPSD
AQIVEAMDGN LCRCGTYQRI KIAIHRAAKE AA
