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Database: UniProt
Entry: I5CQ97_9BURK
LinkDB: I5CQ97_9BURK
Original site: I5CQ97_9BURK 
ID   I5CQ97_9BURK            Unreviewed;       505 AA.
AC   I5CQ97;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Xanthine dehydrogenase small subunit {ECO:0000313|EMBL:EIM98065.1};
GN   ORFNames=WQE_26000 {ECO:0000313|EMBL:EIM98065.1};
OS   Paraburkholderia hospita BS001.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1171375 {ECO:0000313|EMBL:EIM98065.1};
RN   [1] {ECO:0000313|EMBL:EIM98065.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BS001 {ECO:0000313|EMBL:EIM98065.1};
RX   PubMed=22843604; DOI=10.1128/JB.00725-12;
RA   Nazir R., Hansen M.A., Sorensen S., van Elsas J.D.;
RT   "Draft Genome Sequence of the Soil Bacterium Burkholderia terrae Strain
RT   BS001, Which Interacts with Fungal Surface Structures.";
RL   J. Bacteriol. 194:4480-4481(2012).
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:EIM98065.1}.
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DR   EMBL; AKAU01000131; EIM98065.1; -; Genomic_DNA.
DR   AlphaFoldDB; I5CQ97; -.
DR   PATRIC; fig|1171375.3.peg.5364; -.
DR   Proteomes; UP000004980; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004854; F:xanthine dehydrogenase activity; IEA:InterPro.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
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; IPR016208; Ald_Oxase/xanthine_DH-like.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR005107; CO_DH_flav_C.
DR   InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR   InterPro; IPR012175; Xanth_DH_ssu_bac.
DR   InterPro; IPR014307; Xanthine_DH_ssu.
DR   NCBIfam; TIGR02963; xanthine_xdhA; 1.
DR   PANTHER; PTHR45444:SF3; ALDEHYDE OXIDASE_XANTHINE DEHYDROGENASE, MOLYBDOPTERIN BINDING PROTEIN; 1.
DR   PANTHER; PTHR45444; XANTHINE DEHYDROGENASE; 1.
DR   Pfam; PF03450; CO_deh_flav_C; 1.
DR   Pfam; PF00941; FAD_binding_5; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF01799; Fer2_2; 1.
DR   PIRSF; PIRSF036557; XdhA_RC; 1.
DR   SMART; SM01092; CO_deh_flav_C; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR   SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          200..373
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   505 AA;  55421 MW;  8F0CB81CB30124A3 CRC64;
     MSQPIRFYHR NAIREITDAP VTRTVLQYLR EDARCTGTKE GCAEGDCGAC TVVIGERNDA
     GGVSFKTVNA CIQFLPTLDG KALFTVEDLR QPDGSLHPVQ EAMVECHGSQ CGFCTPGFVM
     SMWSMYEKHG HEHSCANRTV PNRADIANAL TGNLCRCTGY RPIIEAAERM FELPAPKAPV
     DVKALAGKLA TLERGETFHY ERNGQQFDAP RTVAALAKIK ADAPATRILA GSTDIGLWVT
     KMMRDLGHIV YVGQIAEMQK LNVTEDWIEI GAGVTVERAY AELAKQYPEL TEMWQRFASL
     PIRNAGTIGG NVANGSPIGD SMPGLIALGA RVVLRGGEIE RELALEDLYL AYQKKDMAEH
     EFVVGVKVPA RNEARKHFQF RTYKISKRFD SDISAVCAAF SFIADGETIR EPRIAFGGMA
     ATPKRATHAE AALADNEWHE ATAQIAMLAL AKDYQPMSDM RATSDYRLEA ATNTLYRFWL
     ETRPNNPLQK SALDVRAVLA AGAAA
//
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