ID A0A3N4UTP2_9BURK Unreviewed; 495 AA.
AC A0A3N4UTP2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Xanthine dehydrogenase small subunit {ECO:0000313|EMBL:RPE65030.1};
GN ORFNames=EDC62_2156 {ECO:0000313|EMBL:RPE65030.1};
OS Tibeticola sediminis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Tibeticola.
OX NCBI_TaxID=1917811 {ECO:0000313|EMBL:RPE65030.1, ECO:0000313|Proteomes:UP000272193};
RN [1] {ECO:0000313|EMBL:RPE65030.1, ECO:0000313|Proteomes:UP000272193}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 101684 {ECO:0000313|EMBL:RPE65030.1,
RC ECO:0000313|Proteomes:UP000272193};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (NOV-2018) 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:RPE65030.1}.
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DR EMBL; RKQL01000005; RPE65030.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4UTP2; -.
DR OrthoDB; 9179439at2; -.
DR Proteomes; UP000272193; 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:UP000272193}.
FT DOMAIN 6..93
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 208..381
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 495 AA; 53414 MW; 61895856347B22C7 CRC64;
MPEVTNTVRF VLDGRIVEAR GVRRTTTVLD YLREHLHRTG TKEGCAEGDC GACVVLVGEL
TEDGQRVRYA PVNSCLQLLP TLDGKSLKTV ESLQGADGRL HPVQEAMVAC HGSQCGFCTP
GIVMSLAGLL QSVAQPGRAE VNDALSGNLC RCTGYRPIVD AALQAAQAPA EALRIDDAAD
LPLLQQIRRA TEPTYSLEGE IVVQPVLRTK KGSEFVAPAT VEELADYLVK NPDATLLAGS
TEIGLKVNKA FLRPARIAYL GHVAELRRVQ TTPEAWQIGA AVPLAEVQTL LADAYPDFAE
VLRRFGSPPI RSTATLAGNI ANGSPIGDSM PCLMALDATL LLRRGRQTRR LPLTQFYTGQ
KRTVLESGEF IEAVVVPRPR AGEVFRAHKV SKRFEQDISA TLFALRYRLV EGRFADVRVA
CNGLAPAPCR VPLIEAVLEG RAPADVTAAE LDAAVAAGFT PRDGLRASWH YRALLARNLV
LQFVEDAAGV EETAR
//
