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Database: UniProt
Entry: A0A2I0G0Z6_9GAMM
LinkDB: A0A2I0G0Z6_9GAMM
Original site: A0A2I0G0Z6_9GAMM 
ID   A0A2I0G0Z6_9GAMM        Unreviewed;       480 AA.
AC   A0A2I0G0Z6;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Xanthine dehydrogenase small subunit {ECO:0000313|EMBL:PKH26602.1};
GN   Name=xdhA {ECO:0000313|EMBL:PKH26602.1};
GN   ORFNames=CIG19_02065 {ECO:0000313|EMBL:PKH26602.1};
OS   Enterobacterales bacterium CwR94.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales.
OX   NCBI_TaxID=2025587 {ECO:0000313|EMBL:PKH26602.1, ECO:0000313|Proteomes:UP000237543};
RN   [1] {ECO:0000313|EMBL:PKH26602.1, ECO:0000313|Proteomes:UP000237543}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CwR94 {ECO:0000313|EMBL:PKH26602.1,
RC   ECO:0000313|Proteomes:UP000237543};
RA   de Groot N.N.;
RL   Submitted (AUG-2017) 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:PKH26602.1}.
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DR   EMBL; NVXY01000001; PKH26602.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I0G0Z6; -.
DR   OrthoDB; 9775084at2; -.
DR   Proteomes; UP000237543; 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:UP000237543}.
FT   DOMAIN          1..85
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          187..360
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   480 AA;  52493 MW;  F4FC0E64D53054E7 CRC64;
     MIQFLYHDRL MTETQCDPNM TVLHWLRRRQ QQTGTKEGCA SGDCGACTVA LGRVVAGRIR
     YESANSCLLP ISQLQGCQLL SVDSLKQSSQ LHPVQQSLAD CHASQCGFCT PGFVMSVFTL
     AKQEIAPDRH AINEALGGNL CRCTGYRPLV EAAIKVCAVP LNDTFLRNEQ QTVQQLQALA
     NPDVQSLNEA GHQLWLPKTV SQLAALYQAN PQAQLIAGGT DLMLQVTQQF RALPALIALH
     QIAELQQCSQ SDDHYIIGAA APITDVAHFL QPMLPAFGRL LQRFASQQIR NLGTCGGNIA
     NASPIGDIPP LLLALDAWLL VQQGEQLRRV ALADFFLDYR KTQLRPGEFI RTIHIPKPAA
     MTQLRAWKVS KRQDDDISTV CGTFNAQFTE GVLRAPRVAF GGMAAIPKRA AGCEAALNGQ
     PLNEQTLEVA CAALTQDFQP LSDFRGSSAY RLAVAQNLLR RYFAALQDHS QPLEVSDDVA
//
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