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Database: UniProt
Entry: W6KF88_MAGSQ
LinkDB: W6KF88_MAGSQ
Original site: W6KF88_MAGSQ 
ID   W6KF88_MAGSQ            Unreviewed;       153 AA.
AC   W6KF88;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Isoquinoline 1-oxidoreductase (Iron-sulfur subunit ) {ECO:0000313|EMBL:CCQ72161.1};
DE            EC=1.3.99.16 {ECO:0000313|EMBL:CCQ72161.1};
GN   Name=iorA {ECO:0000313|EMBL:CCQ72161.1};
GN   ORFNames=MGMAQ_0172 {ECO:0000313|EMBL:CCQ72161.1};
OS   Magnetospira sp. (strain QH-2) (Marine magnetic spirillum (strain QH-2)).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Thalassospiraceae; Magnetospira.
OX   NCBI_TaxID=1288970 {ECO:0000313|EMBL:CCQ72161.1, ECO:0000313|Proteomes:UP000032733};
RN   [1] {ECO:0000313|EMBL:CCQ72161.1, ECO:0000313|Proteomes:UP000032733}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QH-2 {ECO:0000313|EMBL:CCQ72161.1,
RC   ECO:0000313|Proteomes:UP000032733};
RX   PubMed=23841906; DOI=10.1111/1462-2920.12180;
RA   Ji B., Zhang S.D., Arnoux P., Rouy Z., Alberto F., Philippe N., Murat D.,
RA   Zhang W.J., Rioux J.B., Ginet N., Sabaty M., Mangenot S., Pradel N.,
RA   Tian J., Yang J., Zhang L., Zhang W., Pan H., Henrissat B., Coutinho P.M.,
RA   Li Y., Xiao T., Medigue C., Barbe V., Pignol D., Talla E., Wu L.F.;
RT   "Comparative genomic analysis provides insights into the evolution and
RT   niche adaptation of marine Magnetospira sp. QH-2 strain.";
RL   Environ. Microbiol. 16:525-544(2014).
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DR   EMBL; FO538765; CCQ72161.1; -; Genomic_DNA.
DR   RefSeq; WP_046020039.1; NZ_FO538765.1.
DR   AlphaFoldDB; W6KF88; -.
DR   STRING; 1288970.MGMAQ_0172; -.
DR   KEGG; magq:MGMAQ_0172; -.
DR   HOGENOM; CLU_052511_3_0_5; -.
DR   OrthoDB; 7375656at2; -.
DR   Proteomes; UP000032733; 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:SF2; BLR6218 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:CCQ72161.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032733}.
FT   DOMAIN          1..78
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   153 AA;  16381 MW;  734B340630CBA2FC CRC64;
     MRYELKINGQ PRSVDAEPGT PLLWVLRDLL DLTGTKFGCG VAACGSCTVL LAGEPVRSCQ
     TPVEDATTGA IVTIEGANDR IATAVREAWQ EKDVVQCGYC QSGQIMSAIG LLSEIPRPSD
     KEIDAYMDGN VCRCATYVRI KEAIKLASGK LEG
//
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