ID S9RQT2_9RHOB Unreviewed; 468 AA.
AC S9RQT2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Xanthine dehydrogenase {ECO:0000313|EMBL:EPX76369.1};
DE EC=1.17.1.4 {ECO:0000313|EMBL:EPX76369.1};
GN ORFNames=Salmuc_03493 {ECO:0000313|EMBL:EPX76369.1};
OS Salipiger mucosus DSM 16094.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salipiger.
OX NCBI_TaxID=1123237 {ECO:0000313|EMBL:EPX76369.1, ECO:0000313|Proteomes:UP000015347};
RN [1] {ECO:0000313|Proteomes:UP000015347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16094 {ECO:0000313|Proteomes:UP000015347};
RX PubMed=25197501; DOI=10.4056/sigs.4909790;
RA Riedel T., Spring S., Fiebig A., Petersen J., Kyrpides N.C., Goker M.,
RA Klenk H.P.;
RT "Genome sequence of the exopolysaccharide-producing Salipiger mucosus type
RT strain (DSM 16094(T)), a moderately halophilic member of the Roseobacter
RT clade.";
RL Stand. Genomic Sci. 9:1331-1343(2014).
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:EPX76369.1}.
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DR EMBL; APVH01000052; EPX76369.1; -; Genomic_DNA.
DR RefSeq; WP_020043572.1; NZ_KE557283.1.
DR AlphaFoldDB; S9RQT2; -.
DR STRING; 1123237.Salmuc_03493; -.
DR eggNOG; COG4630; Bacteria.
DR HOGENOM; CLU_001681_9_0_5; -.
DR OrthoDB; 9792018at2; -.
DR Proteomes; UP000015347; 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:UniProtKB-EC.
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,
KW ECO:0000313|EMBL:EPX76369.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015347}.
FT DOMAIN 1..82
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 176..349
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 165..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 468 AA; 50727 MW; 1694748E2A3BE1B1 CRC64;
MDISFLLNGE KIELRGVDPT RTALDWLREE RGLTGTKEGC NEGDCGACSV MVTDGAGTKA
LNACILFLPQ LHGKALRTVE GLSGPGGEMH PVQKAMVEHH GSQCGFCTPG FVVAMAAAHL
NGDRNHDDAL AGNLCRCTGY APIVRAAEAA AQVDVPRWLD DDPAVALAGD DEAPDTGGPA
PRGHAPESVD ELAELAARHP EATLVAGATD VGLWVTKDLR ELPEMIFLNR CRDLQQIEVG
DDEIRIGAGV TMDRVLELMR EHHPSYAQML RRYGAGQVRA AATIGGNIAN GSPIGDNPPP
LIALGARLHL RYRDTRREMA LEHFFLDYGK QDRHPGEIVE AVTIPRQADR LRVYKLSKRL
DQDISAVCGA FSVRVEGGTV QEARIAFGGM AATPKRASHV EAALTGRPWS DEALVAAWDE
WELDFAPMSD MRASAEYRLN AARNMLTRYL LTDLGAETDV RAIHEVRP
//
