ID   A0A1D7XHH3_9CLOT        Unreviewed;       855 AA.
AC   A0A1D7XHH3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Selenium-dependent xanthine dehydrogenase {ECO:0000313|EMBL:AOR22808.1};
GN   Name=xdh {ECO:0000313|EMBL:AOR22808.1};
GN   ORFNames=BGI42_03370 {ECO:0000313|EMBL:AOR22808.1};
OS   Clostridium taeniosporum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=394958 {ECO:0000313|EMBL:AOR22808.1, ECO:0000313|Proteomes:UP000094652};
RN   [1] {ECO:0000313|Proteomes:UP000094652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1/k {ECO:0000313|Proteomes:UP000094652};
RA   Walker J.R.;
RT   "Genomics of Clostridium taeniosporum, an organism which forms endospores
RT   with ribbon-like appendages.";
RL   Submitted (SEP-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; CP017253; AOR22808.1; -; Genomic_DNA.
DR   RefSeq; WP_069678968.1; NZ_CP017253.2.
DR   AlphaFoldDB; A0A1D7XHH3; -.
DR   STRING; 394958.BGI42_03370; -.
DR   KEGG; ctae:BGI42_03370; -.
DR   OrthoDB; 9759099at2; -.
DR   Proteomes; UP000094652; 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: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   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; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000094652}.
FT   DOMAIN          1..74
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   855 AA;  93459 MW;  C23EA66A880B932A CRC64;
     MFKLNINGKD VISKIDKSLL SFLRDDLRIT SVKDGCSEGA CGTCTVLVDG KKVKACIQKV
     SKFVGKKILT VEGLSCREKE VYEHCFAEAG AVQCGFCIPG MVICAKALLD VNLNPTRLDV
     KKAINGNICR CTGYKKIEEA ILMAAEYFRN NIKIIPNSTE LKMAQRFKRV DAAEKVNGTG
     IFVDDIELQG MIYAKAVHSK YPRAIINKID ISKAEAHPDC VKILLAKDVP NNIIGHIKQD
     WDVLIAEGQT TRYIGDALAL VATYHKDKLD EVCGLVEVDY TELEPVTSPT DALRSDAPLI
     HVDGNIMSRS MLQRGNATEA IKNSKYVVTR KYQTPYQEHG FMEPECAIAM PEGEDGILLY
     TSSQSVYDEQ REISNMLKIP IEKVHSHSQL VGGGFGGKED MSVQHHAALM AWYTKKPVKV
     KFSRQESLNY HTKRHPMGIE MTTACDENGY LTAMKAVIIA DTGAYASLGG PVLERACTHA
     GGPYNYQNMD ILGMSVYTNN VVSGAFRGFG AAQSCFATES NINLLAEMVG ISPWEIRYRN
     AIRPGQVLPN GQIADESVAI AECLEAVKDV YESNSYAGIA IGWKNSGTGV GHKDIGRCIL
     SIEHGKVHIR TSAACMGQGI AQMCTTVLCE TTGLDPALII HERPDTVRTP NSGTSTASRQ
     TVVTGEAVRR VSEKLKVELD KGLKLDDLEG REFYGEYSAK TDPMGAIKDN PISHVSYSYG
     AQVIVLNEEG KVVKAVAGFD VGTPVNIQSV EGQIEGGMIM GLGYALTEEF KVERGYPKIK
     LGTLGLIRAK DAPELEVILV QGKGKIPQTY GAKGCGELCL IPTAPACAHA YYRLDGKFRN
     QLPLRDTFYK RSKNK
//