ID   A0A1I5S3H6_9BRAD        Unreviewed;       906 AA.
AC   A0A1I5S3H6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=CO or xanthine dehydrogenase, Mo-binding subunit {ECO:0000313|EMBL:SFP65284.1};
GN   ORFNames=SAMN05216330_10916 {ECO:0000313|EMBL:SFP65284.1};
OS   Bradyrhizobium sp. Ghvi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1855319 {ECO:0000313|EMBL:SFP65284.1, ECO:0000313|Proteomes:UP000198509};
RN   [1] {ECO:0000313|EMBL:SFP65284.1, ECO:0000313|Proteomes:UP000198509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ghvi {ECO:0000313|EMBL:SFP65284.1,
RC   ECO:0000313|Proteomes:UP000198509};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006849}.
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DR   EMBL; FOVU01000009; SFP65284.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5S3H6; -.
DR   STRING; 1855319.SAMN05216330_10916; -.
DR   OrthoDB; 9763985at2; -.
DR   Proteomes; UP000198509; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1.
DR   Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 4.
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; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR   InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR   InterPro; IPR016208; Ald_Oxase/xanthine_DH-like.
DR   InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1.
DR   InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2.
DR   InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   PANTHER; PTHR11908:SF132; ALDEHYDE OXIDASE 1-RELATED; 1.
DR   PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR   Pfam; PF01315; Ald_Xan_dh_C; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF01799; Fer2_2; 1.
DR   Pfam; PF02738; MoCoBD_1; 1.
DR   Pfam; PF20256; MoCoBD_2; 1.
DR   SMART; SM01008; Ald_Xan_dh_C; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR   SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR   SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          1..74
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   906 AA;  96580 MW;  5C0CF7FDFD38A32E CRC64;
     MSFEINGTTF PQAPRAGQCL RTFLRELGHF GVKKGCDAGD CGACTVLLDG EPVHSCLIPA
     FRAEGRPITT IEGLGGEHAH QMQQAFLDAQ GFQCGFCTAG MILTCASLNQ AQRTDLDAAL
     KGNICRCTGY RSIEDAIHGK INVEESVEAG GAFGRSLPAP AGPDVVRGQA RYTFDTKVDN
     FLHIKLLRSP HAHARLVAID RSAAMAVAGV HAILTHEDAP SVLFSTARHE KDWMDPEDTR
     VLDDVVRFIG QKVAAVVAES EAAAEEACRR LKIEYEILPA LIDPEQAMMP GAPRVHPDRT
     TANRVADAQR NLVAEIHGEF GDVASALAAS AVTYEGTFHS HRVQHAALET HGGLAWLDAT
     GVLNVRTSTQ VPFLTRRALS GIFGLPIDKV RVFCERVGGG FGGKQEMFVE DILALAALKT
     GRPVKLELTR EEQFIATSTR HPMRVHIRAG ADAEGKLTAL QLDVLSNTGA YGNHGPSVMF
     HAVSESIAVY NCPNKRVDGF VVYTNTVPAG AFRGYGLPQA VIAVEAAIDE LARQLGISPY
     DMRRRNIIRQ GDPMLSPPES EYHDVLYGSY GLDQCIDLVE HAMQADQPPE LSPEWLTGDG
     IALTMIDTVP PAGHIADATA TLNDDGGFEL TVGTAEFGNG TSTVHRQIAA TVLATTVDRI
     RLRQSDTAHG GHDTGAYGST GLFVAGKATQ AAATQLATEL KAAAAGAWLC DAATCTLEDE
     FVVSGVRRMS FVELARLARE GGRPLAGHGN SEGSPRSVGF NVQGFRVAVN KGTGEVRILR
     SVQAADAGVV ANPMQCRGQV EGGVAQALGA ALYEEMVIDA QGRVTNPKFR DYHLPSFADV
     PRTEVFFAET SDTIGPLGAK SMSESPYNPV AAALGNAIAD ATGIRFTAPP FKPDRLFPAL
     HDKFGG
//