ID J2T352_9PSED Unreviewed; 484 AA.
AC J2T352;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Xanthine dehydrogenase, small subunit {ECO:0000313|EMBL:EJM68734.1};
GN ORFNames=PMI30_01175 {ECO:0000313|EMBL:EJM68734.1};
OS Pseudomonas sp. GM50.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144332 {ECO:0000313|EMBL:EJM68734.1, ECO:0000313|Proteomes:UP000007513};
RN [1] {ECO:0000313|EMBL:EJM68734.1, ECO:0000313|Proteomes:UP000007513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM50 {ECO:0000313|EMBL:EJM68734.1,
RC ECO:0000313|Proteomes:UP000007513};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJM68734.1}.
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DR EMBL; AKJK01000040; EJM68734.1; -; Genomic_DNA.
DR RefSeq; WP_008007010.1; NZ_AKJK01000040.1.
DR AlphaFoldDB; J2T352; -.
DR PATRIC; fig|1144332.3.peg.1122; -.
DR Proteomes; UP000007513; 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.
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; PTHR11908:SF132; ALDEHYDE OXIDASE 1-RELATED; 1.
DR PANTHER; PTHR11908; 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..90
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 192..365
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 484 AA; 53183 MW; 28915A8531F2C111 CRC64;
MIQFLLNQEL RSEHALDPNL TVLNYLREHV GKPGTKEGCA SGDCGACTVV VGELQTDDDS
REHIRYRSLN SCLTFVSSLH GKQLISVEDL KHQGELHSVQ KAMVECHGSQ CGFCTPGFVM
SLFALQKNSD QPDAHKAHEA LAGNLCRCTG YRPILAAAEQ SCCGKQPDQF DAREVETIAR
LKAIAPTDIG ELNSGDKRCL VPLTVADLAD LYDAYPQARL LAGGTDLALE VTQFHRTLPV
MIYVGNVAEM KRIERFDDRL EIGAATALSD CYEALKAEYP DFGELLQRFA SLQIRNQGTL
GGNIGNASPI GDSPPLLIAL GAQIVLCKGE TRRTMALEDY FIDYRVTARQ ESEFIEKIIV
PRASVEQLFR AYKVSKRLDD DISAVCAAFN LRIDTGVIAD ARVAFGGMAA IPKRAKNCEA
ALLGAPFNNA TLERACAALA EDFTPLSDFR ASKEYRLLSA QNLLRKYFIE LQTPHIETRV
TAYV
//