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Database: UniProt
Entry: A0A1G8WY19_9GAMM
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ID   A0A1G8WY19_9GAMM        Unreviewed;       483 AA.
AC   A0A1G8WY19;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Xanthine dehydrogenase small subunit {ECO:0000313|EMBL:SDJ83113.1};
GN   ORFNames=SAMN04487954_108140 {ECO:0000313|EMBL:SDJ83113.1};
OS   Halomonas gudaonensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=376427 {ECO:0000313|EMBL:SDJ83113.1, ECO:0000313|Proteomes:UP000198525};
RN   [1] {ECO:0000313|EMBL:SDJ83113.1, ECO:0000313|Proteomes:UP000198525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.6133 {ECO:0000313|EMBL:SDJ83113.1,
RC   ECO:0000313|Proteomes:UP000198525};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNES01000008; SDJ83113.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8WY19; -.
DR   STRING; 376427.SAMN04487954_108140; -.
DR   OrthoDB; 9775084at2; -.
DR   Proteomes; UP000198525; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198525}.
FT   DOMAIN          1..85
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          180..359
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   483 AA;  52535 MW;  790AD6FD36701279 CRC64;
     MIDFLLNGQP RHCAASPDTS VLEMLRENLG QTGTKEGCAS GDCGACTVAI GETDADGRLH
     YRSANACITP AHQLNGRHLV TVEGLADGDD LHPAQAAMVA CHGSQCGFCT PGIVMSLFTL
     HEAQRGGDLA PLTPQRLEAA LGGNLCRCTG YRPIRDAALT MTEHPERRPQ WLDAAAPRPA
     APSSDAPFAQ PETLAELVEL RRRHPEARLV AGATDLWLEV TQRLTRFERL IDVTRVAELN
     AIEETTLDDG RHGWWIGAAV TYARLEPLLE ENVEPFAHLL HRLGSAQIRN RGTLGGNIAN
     ASPIGDTPPV LLALGSRLWL AGPEGERELP LDDFFLGYKQ TALREGETIR AVFLPRPEAE
     CHLKVWKLSK RREDDISAVL GAFAWQLEAG ILRNVRLAFG GMAATPKRAA QAEAALEGQP
     PTAAAFRAAR QALGDDFQPM SDVRGSDHYR QLSAANLLER LRLVIAKQDS DTSREVMLHA
     YAH
//
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