ID A0A1Y4NY52_9FIRM Unreviewed; 864 AA.
AC A0A1Y4NY52;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Selenium-dependent xanthine dehydrogenase {ECO:0000313|EMBL:OUP85734.1};
GN ORFNames=B5F07_03455 {ECO:0000313|EMBL:OUP85734.1};
OS Lachnoclostridium sp. An169.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1965569 {ECO:0000313|EMBL:OUP85734.1, ECO:0000313|Proteomes:UP000195962};
RN [1] {ECO:0000313|Proteomes:UP000195962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An169 {ECO:0000313|Proteomes:UP000195962};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00006849}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OUP85734.1}.
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DR EMBL; NFKT01000003; OUP85734.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4NY52; -.
DR OrthoDB; 9759099at2; -.
DR Proteomes; UP000195962; 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 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; 5.
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 Reference proteome {ECO:0000313|Proteomes:UP000195962}.
FT DOMAIN 3..77
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 864 AA; 93397 MW; A8E3358F43B3CDE9 CRC64;
MKAEYSFTVN GVLRSTDVDK PLLRYLRDDL HLHSVKDGCS EGACGTCTII VDGKAVKSCV
LTTKRAAGKN IITTEGLSER EKETFVYAFG SKGAVQCGFC IPGMVMAGKA LIDRNPDPTE
EEIKAALKGN ICRCTGYKKI IEGIRLAAAI LRGDAKIEES LEKGETYGVG EKAFRLDVRE
KVLGYGEYPD DVEMEGMVYA SAVRSRYARA KVLDIRAEKA LALPGVLAVL TADDVPNNKV
GHLQQDWDVM IAKGNITRCV GDAICLVVAE SREILEEAKK LVSIDYEELT PVTSIRQAMA
ADAPKVHSGG NLCQSRHVTR GDAKKALENS RYVVTKTYRT PFTEHAFLEP ECAVAFPYKG
GVKVLSSDQG VYDTRKEISI MFGWEPERIV VENKLVGGGF GGKEDVSAQH IAALAAVKVN
RPVKVVFSRQ ESINFHPKRH AMEGTFTLGC DENGIFTGLD CEIYFDTGAY ASLCGPVLER
ACTHSVGPYC YQNTDIRGYG YYTNNPPAGA FRGFGVCQSE FALESNINLL AEMVGISPWE
IRYRNAIEPG KVLPNGQIAD CSTALKETLL AVKDVYEANP GRAGIACAMK NAGVGVGLPD
KGRAKLVVHD GKVELYSAAS DIGQGCATVL VQMVSETTGL GREMIRNMGA NSEVAPDSGT
TSGSRQTLIT GEAVRMAAAQ LDEELKKAGG DLSKLEGREF FAEFFDPTDK LGADVPNPKS
HVAYGFATHV VILDDDGRVK EVYAAHDSGK VVNPISIQGQ IEGGVLMGLG YALTEDFPLK
DGVPQARYGT LGLMRATQIP DIHAIYVEKE ELLPFAYGAK GIGEIATIPT APAVQGAYYA
MDHVLRTKLP MENTYYSKKK KAVK
//
