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Database: UniProt
Entry: A0A0P7Y596_9RHOB
LinkDB: A0A0P7Y596_9RHOB
Original site: A0A0P7Y596_9RHOB 
ID   A0A0P7Y596_9RHOB        Unreviewed;       460 AA.
AC   A0A0P7Y596;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Xanthine dehydrogenase FeS/FAD binding subunit XdhA {ECO:0000313|EMBL:KPQ15511.1};
GN   Name=xdhA {ECO:0000313|EMBL:KPQ15511.1};
GN   ORFNames=HLUCCO18_11870 {ECO:0000313|EMBL:KPQ15511.1};
OS   Rhodobacteraceae bacterium HLUCCO18.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=1666917 {ECO:0000313|EMBL:KPQ15511.1, ECO:0000313|Proteomes:UP000050333};
RN   [1] {ECO:0000313|EMBL:KPQ15511.1, ECO:0000313|Proteomes:UP000050333}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLUCCO18 {ECO:0000313|EMBL:KPQ15511.1};
RA   Nelson W.C., Romine M.F., Lindemann S.R.;
RT   "Identification and resolution of microdiversity through metagenomic
RT   sequencing of parallel consortia.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:KPQ15511.1}.
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DR   EMBL; LJSY01000027; KPQ15511.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7Y596; -.
DR   STRING; 1666917.HLUCCO18_11870; -.
DR   PATRIC; fig|1666917.4.peg.1145; -.
DR   Proteomes; UP000050333; 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; PS51085; 2FE2S_FER_2; 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          1..81
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          171..344
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   460 AA;  49140 MW;  1A501DF4AF80EEDE CRC64;
     MTIRFLLNGE PQAVDAPPTT TLLDWLRETR GLTGTKEGCN EGDCGACTVM VTDETGARAL
     NACILFLPQL DGRAVRTVEG IAGPDGALHP VQQAMVEHHG SQCGFCTPGF IVSMATAHLN
     GRTDFDNQLA GNLCRCTGYA PIIRAAEAAA LVPVPDWMEA DAEMLDLLAH DVPAGSEIAL
     PRSADALAEW YDAHPDATLI AGATDVGLWV TKNLRDLAPV AFLNQCDDLK GIVSDKETIR
     IGAMTSLTEL GDFIADRHPS FAEMIRRYGS VQVRNAATVG GNIANGSPIG DSPPALIALG
     AALHLRKGDT RRALPLEEFF LDYGKQDRAP GEFVEAVSVP VQPDRLRVYK LSKRFDQDIS
     AVCGAFSITV EDGTVTQARI AFGGMAGTPK RASTVEAALV GQPWARASVD AARARFAEDF
     TPLSDMRASA AYRLETASNM LLRYFGEMSG QPVSVLEVRP
//
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