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Database: UniProt
Entry: Q2L204_BORA1
LinkDB: Q2L204_BORA1
Original site: Q2L204_BORA1 
ID   Q2L204_BORA1            Unreviewed;       173 AA.
AC   Q2L204;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   24-JAN-2024, entry version 101.
DE   SubName: Full=Isoquinoline 1-oxidoreductase alpha subunit {ECO:0000313|EMBL:CAJ49146.1};
DE            EC=1.3.99.16 {ECO:0000313|EMBL:CAJ49146.1};
GN   Name=iorA {ECO:0000313|EMBL:CAJ49146.1};
GN   OrderedLocusNames=BAV1533 {ECO:0000313|EMBL:CAJ49146.1};
OS   Bordetella avium (strain 197N).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910 {ECO:0000313|EMBL:CAJ49146.1, ECO:0000313|Proteomes:UP000001977};
RN   [1] {ECO:0000313|EMBL:CAJ49146.1, ECO:0000313|Proteomes:UP000001977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=197N {ECO:0000313|EMBL:CAJ49146.1,
RC   ECO:0000313|Proteomes:UP000001977};
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA   Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA   Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA   Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT   with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT   extensive diversity in surface structures associated with host
RT   interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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DR   EMBL; AM167904; CAJ49146.1; -; Genomic_DNA.
DR   RefSeq; WP_012417210.1; NC_010645.1.
DR   AlphaFoldDB; Q2L204; -.
DR   STRING; 360910.BAV1533; -.
DR   GeneID; 41393397; -.
DR   KEGG; bav:BAV1533; -.
DR   eggNOG; COG2080; Bacteria.
DR   HOGENOM; CLU_052511_3_0_4; -.
DR   OMA; VNGRWRE; -.
DR   OrthoDB; 9179439at2; -.
DR   Proteomes; UP000001977; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0047121; F:isoquinoline 1-oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 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   PANTHER; PTHR44379:SF6; BLR6046 PROTEIN; 1.
DR   PANTHER; PTHR44379; OXIDOREDUCTASE WITH IRON-SULFUR SUBUNIT; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF01799; Fer2_2; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:CAJ49146.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001977}.
FT   DOMAIN          9..85
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   173 AA;  18433 MW;  74F995D7ACD4EA1F CRC64;
     MASSLSTASA IRLMVNGCTH DVPASADTAL LHVLRNDLEL NGPKYGCGLG ECGACTVLID
     GVAARSCVIP VKAAQGRAVT TLEGLGRRQA PGPTQQAFIE CQAAQCGYCL NGMIMTVEAL
     LRRNPRPTEH MLRNELHHNL CRCGTHVEIM QAALRAVQLR AETGAQSADE ARR
//
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