ID   IORB_BREDI              Reviewed;         781 AA.
AC   Q51698;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Isoquinoline 1-oxidoreductase subunit beta;
DE            EC=1.3.99.16;
GN   Name=iorB;
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; CAA88754.1; -; Genomic_DNA.
DR   PIR; B56939; B56939.
DR   AlphaFoldDB; Q51698; -.
DR   SMR; Q51698; -.
DR   KEGG; ag:CAA88754; -.
DR   BioCyc; MetaCyc:MON-20839; -.
DR   BRENDA; 1.3.99.16; 982.
DR   GO; GO:0047121; F:isoquinoline 1-oxidoreductase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR   InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR   InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
DR   InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR   InterPro; IPR012368; OxRdtase_Mopterin-bd_su_IorB.
DR   InterPro; IPR006311; TAT_signal.
DR   Pfam; PF02738; Ald_Xan_dh_C2; 3.
DR   PIRSF; PIRSF036389; IOR_B; 1.
DR   SMART; SM01008; Ald_Xan_dh_C; 1.
DR   SUPFAM; SSF54665; SSF54665; 1.
DR   SUPFAM; SSF56003; SSF56003; 2.
DR   PROSITE; PS51318; TAT; 1.
PE   1: Evidence at protein level;
KW   Oxidoreductase.
FT   CHAIN           1..781
FT                   /note="Isoquinoline 1-oxidoreductase subunit beta"
FT                   /id="PRO_0000084216"
SQ   SEQUENCE   781 AA;  84483 MW;  45F9B3AEC7AA4F57 CRC64;
     MKTVLPSVPE TVRLSRRGFL VQAGTITCSV AFGSVPAAAG DTAESTPSIA AVSPNVWVRV
     HADGIVDIVC PAVELGQGAH TALPRFVAEE LDADWDRVRV QQAGASDKVY GNPLAWGTQF
     TAASRTTVGY FDVLRVAGAQ ARFVLVQTAA RRWSVPADQL ETQKGVVLHR RSRRSATYGE
     LVASVQVPES FPHFFARNEA TQPADDYFGA APPSVVAQAA GPASGAIALK HRSTYRLIGK
     DAPRKDIPPK VNGQACYGMD VQVPGMLYAM VETGPVAGMA PERVDDGAAR QVPGIHHVLS
     LPHGVAVVGR DIFAVRAARA RLLVNWKANP DKQSYDSGQV LDEFSDLCRN GIERNAVQAW
     KQGELSSIDA VFARPDVRIE SFEMQSDLVY QAPMEPQSAV IQPHADGSAE AWVGTQWPTV
     EQGFAAGILG IAPDKLTMHL PLVGGGFGRR LEPGALVDAA HIVRAIGKTV KVIWSREDDL
     KRNPFRQALA CRVEAAVLEK DQRILALRHT VAADSWLARL FPQYFNAYQQ TDPGNWIGGM
     VAYDVPLQRI DALTPRRSVD VCYMRGIGVA QVKFAQESLV DQIARRLNAD PVDFRLAHLN
     TSPRGAAVVR TVAEMSDWKR RSADAGGGMA LGLAYTPYSN AHVALVSEVH FNRSENTLSV
     SRVWCAVDVG MVAQPDIVKA QMEGGIIQGL SVALMERVQV AKGVLQHSNF HDYPMLRMSQ
     VPQIHVRLVE TDQAMAGVAE LGLLQIGPAI NNAFARITGQ HLRSLPMRPA LAQMKRSGPT
     A