ID A0A1L9QJS2_9CYAN Unreviewed; 465 AA.
AC A0A1L9QJS2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Xanthine dehydrogenase small subunit {ECO:0000313|EMBL:OJJ15114.1};
GN ORFNames=BI308_24580 {ECO:0000313|EMBL:OJJ15114.1};
OS Roseofilum reptotaenium AO1-A.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Desertifilales; Desertifilaceae;
OC Roseofilum.
OX NCBI_TaxID=1925591 {ECO:0000313|EMBL:OJJ15114.1, ECO:0000313|Proteomes:UP000183940};
RN [1] {ECO:0000313|EMBL:OJJ15114.1, ECO:0000313|Proteomes:UP000183940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AO1-A {ECO:0000313|EMBL:OJJ15114.1};
RA Buerger P., Wood-Charlson E.M., Weynberg K.D., Willis B., Van Oppen M.J.;
RT "CRISPR-Cas defence system in Roseofilum reptotaenium: evidence of a
RT bacteriophage-cyanobacterium arms race in the coral black band disease.";
RL Submitted (OCT-2016) 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:OJJ15114.1}.
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DR EMBL; MLAW01000073; OJJ15114.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9QJS2; -.
DR STRING; 1925591.BI308_24580; -.
DR Proteomes; UP000183940; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000183940}.
FT DOMAIN 2..87
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 178..351
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 465 AA; 51042 MW; 556052521DF210E4 CRC64;
MTQPYLIVNN KTLFLKDTSP HSTLLEYLRQ SGFVGTKEGC GDGDCGACTV AIIAQNQEGK
PYYQAINSCI VPLGAVIGRE IITVEGIAGE TLHPVQQAMV ETGGSQCGYC TPGFIMSMFC
AYYQGTVNDV CIEGNLCRCT GYLPIRRAAQ QVTGATNIQD RFTQKLETAS TVIIECEYGA
DGDRFHRPIN LNQLLHLLQQ HPNATLIAGA TDIGLHLSHH TQHFPLLISL EAIPELQTLH
ITPESVEIGA ALPLSHIQTH LQGIFPSLDT MLIWFAARQI RNRATLGGNL GTASPIGDLS
PVLLSLDATL SLASPQGERT LPLCNFFQNY RQTALQAGEI IRSISIPRTL PPKAIRRLSQ
SYKVGKRGTD DISIVAAAFT IDLDENHHII HARLAYGGVA PLPIRATQVE DMLIGKLWHL
DTIRDIKPIL QQTFSPLTDL RASAEYRQLL VANLFEKFFH EIECD
//
