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Database: UniProt
Entry: D4LU41_9FIRM
LinkDB: D4LU41_9FIRM
Original site: D4LU41_9FIRM 
ID   D4LU41_9FIRM            Unreviewed;       860 AA.
AC   D4LU41;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Selenium-dependent molybdenum hydroxylase 1 {ECO:0000313|EMBL:CBL24299.1};
DE            EC=1.17.1.4 {ECO:0000313|EMBL:CBL24299.1};
GN   ORFNames=CK5_30730 {ECO:0000313|EMBL:CBL24299.1};
OS   Blautia obeum A2-162.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX   NCBI_TaxID=657314 {ECO:0000313|EMBL:CBL24299.1, ECO:0000313|Proteomes:UP000008955};
RN   [1] {ECO:0000313|EMBL:CBL24299.1, ECO:0000313|Proteomes:UP000008955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A2-162 {ECO:0000313|EMBL:CBL24299.1,
RC   ECO:0000313|Proteomes:UP000008955};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Ruminococcus obeum A2-162.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL24299.1, ECO:0000313|Proteomes:UP000008955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A2-162 {ECO:0000313|EMBL:CBL24299.1,
RC   ECO:0000313|Proteomes:UP000008955};
RA   Pajon A.;
RL   Submitted (MAR-2010) 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; FP929054; CBL24299.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4LU41; -.
DR   KEGG; rob:CK5_30730; -.
DR   PATRIC; fig|657314.3.peg.2947; -.
DR   HOGENOM; CLU_001681_2_3_9; -.
DR   Proteomes; UP000008955; Chromosome.
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:0004854; F:xanthine dehydrogenase activity; IEA:UniProtKB-EC.
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   InterPro; IPR017697; Xdh.
DR   NCBIfam; TIGR03311; Se_dep_XDH; 1.
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,
KW   ECO:0000313|EMBL:CBL24299.1}.
FT   DOMAIN          1..74
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   860 AA;  94046 MW;  D2981D4756AFEB47 CRC64;
     MARFKVNGRT VQTEKNQKLL RFLRDELHLT SVKDGCSEGA CGACTVIIDG KACKACVPDT
     DSLDGREVIT VEGLTEWEKQ VYTYAYGKAG AVQCGFCIPG MVMCTKVLLD VNKTPSDDEI
     RYALRNNYCR CTGYVKIMDA VRLAAKILDT GVIPDDGDQN WTLGNRVSRI DVEEKVLGTG
     RYPDDFYLDG MLYGTALRSK YARARVLSID TSKARALEGV EAVVTAEDIP GENKIGHLKH
     DQYTLIPVGG LTHYLGDAIA LVAAQDRETA EKAKKLIKVE YEVLPPVHTI EEAAAPDAYK
     VFDEEENNIC AHKHISRGNA EEAIQNSKYV ISHHFETPWT EHAFLEPECA VAFYDEDGDV
     FIYSTDQSAH QTLHECSLVL GTDKVKVQNA LVGGGFGGKE DMTVQHLAAL LTYVTKKPVK
     VKLTRAESLL VHPKRHPFYM DMTMGCDEHG NIMGVKATVV SDTGAYASLG GPVLERACTH
     AAGPYHYENF EIEGTAYYTN NPPAGAFRGF GVTQTCFATE TLLNMMADRV GITPWEIRYR
     NAIHPGEVLP NGQIVDESTG LIETLEAVRE DYEAALAEGK PVGIGCAMKN AGVGVGIPDT
     GRVKLIVEDD EKLHIYSGAS CIGQGLGTVL VQMVVTNTDL KHQDIVYERS NTWIAPDSGT
     TSGSRQTLIT GEACRRACEK LMEDRKSGKS LSDMKGKVYY GEYLAKTDPL GANVPNPVSH
     VAYGYATQMC ILDKKTGELE HIVAAHDVGK AVNPLSCEGQ IEGGVVMSMG YALREKYPID
     ENCRPIQKYG SLGLFRSHEV PKIKAIVVDK PGLNVACGAI GIGEITSIPT APAIADAYFR
     YDGIRRYSLP LTDTPYERKW
//
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