ID A0A1F3K7P5_9BACT Unreviewed; 852 AA.
AC A0A1F3K7P5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Selenium-dependent xanthine dehydrogenase {ECO:0000313|EMBL:OFY24564.1};
GN ORFNames=A2W98_08385 {ECO:0000313|EMBL:OFY24564.1};
OS Bacteroidetes bacterium GWF2_33_38.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1797342 {ECO:0000313|EMBL:OFY24564.1, ECO:0000313|Proteomes:UP000177621};
RN [1] {ECO:0000313|EMBL:OFY24564.1, ECO:0000313|Proteomes:UP000177621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OFY24564.1}.
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DR EMBL; MEOF01000012; OFY24564.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F3K7P5; -.
DR STRING; 1797342.A2W98_08385; -.
DR Proteomes; UP000177621; Unassembled WGS sequence.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; 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 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; 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; PS51085; 2FE2S_FER_2; 1.
PE 3: Inferred from homology;
FT DOMAIN 1..77
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 852 AA; 93039 MW; 3436D1536E2D8B0E CRC64;
MITFKLNGKE TKFDGNVELS LLNYLRNELD ITSVKDGCSG QSACGACMVE IDGKAKLSCV
TKLGKLEGAD VTTMEGIPEA VKKVIASAFV EKGAVQCGFC TPGFIMRTKV LLQDNPTPSK
DEIKKALTLN LCRCTGYHKI IESIELAALS LKDNKTVEIT KTDGKIGRRQ SKYEAYETAI
GQRKFVDDYK FEGMLHAALK LSDYPRAKVL KVDTSAAEKL QGVVKIFTAK DIPASQRVGL
IYQDWPMMIK ENEITRYIGD VIASVVAENQ EIARKAVELI KVDYEVLEPV TSVHEAIKEK
IKVHPDHDNL LGNCIIKIGN AEETLKNSKY TAKGTFQTQR IEHAFIETEA AVALPEGNDG
ILLYSQSQGV YEDQKQIAKM LGISEEKVRV ILVANGGGFG GKEDMTVQGH TAMFAWVLKR
PVKLSLSREE SITMHPKRHP IYMEIEVGSD EKGKLTAVKL RAMGDTGAYA SVGTKVMERV
AGHCTGGMFV PVIDIEARTV YTNNIPSGAM RGFGANQVAF AFEACLDEIC LKAGFDRWQF
RYDNALVDGL RTSTGQKLEG VGIRESLLAV KDKFQKAKYA GIATAIKNCG VGNGMADFSD
VIIEILSPTH VRLHHGWTEM GQGVHTVALQ VLCEETGINP DFIEVIVDTK AGIKTGMTTS
SRGTTLVGNA IIDACKTLKV DLKNNDLSKL VGKSYKGHWI CDWTTKPGDP NVKEHITHYA
YGYAAQVAIL DENGEISEIV AAHDAGKIFN PKMFEGQIEG AVHMGVGFAL TEDLPMKDGY
LVSKKLRDCG VLRAHETPNV DVIGIEVKDP VGPYGSKGVG EIGLIPTAAA IANALFMFDG
KRRTELPMKR KK
//
