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
//