ID   A0A370AUN7_9SPIO        Unreviewed;       961 AA.
AC   A0A370AUN7;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Molybdopterin-dependent oxidoreductase Mo/Fe-S-binding subunit {ECO:0000313|EMBL:RDG33337.1};
GN   ORFNames=DV872_04585 {ECO:0000313|EMBL:RDG33337.1};
OS   Oceanispirochaeta sp. M1.
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC   Oceanispirochaeta.
OX   NCBI_TaxID=2283433 {ECO:0000313|EMBL:RDG33337.1, ECO:0000313|Proteomes:UP000253869};
RN   [1] {ECO:0000313|EMBL:RDG33337.1, ECO:0000313|Proteomes:UP000253869}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1 {ECO:0000313|EMBL:RDG33337.1,
RC   ECO:0000313|Proteomes:UP000253869};
RA   Yadav S., Villanueva L., Damste J.S.S.;
RT   "Draft genome sequence of Oceanispirochaeta sp. strain M1.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006849}.
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:RDG33337.1}.
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DR   EMBL; QQPQ01000005; RDG33337.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A370AUN7; -.
DR   OrthoDB; 9759099at2; -.
DR   Proteomes; UP000253869; Unassembled WGS sequence.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1.
DR   Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 4.
DR   InterPro; IPR002888; 2Fe-2S-bd.
DR   InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR   InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR   InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR   InterPro; IPR016208; Ald_Oxase/xanthine_DH-like.
DR   InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1.
DR   InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2.
DR   InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR017699; Mo-bd_YgfN/XdhD.
DR   NCBIfam; TIGR03313; Se_sel_red_Mo; 1.
DR   PANTHER; PTHR11908:SF132; ALDEHYDE OXIDASE 1-RELATED; 1.
DR   PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR   Pfam; PF01315; Ald_Xan_dh_C; 1.
DR   Pfam; PF01799; Fer2_2; 1.
DR   Pfam; PF02738; MoCoBD_1; 1.
DR   Pfam; PF20256; MoCoBD_2; 1.
DR   SMART; SM01008; Ald_Xan_dh_C; 1.
DR   SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR   SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR   SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000253869}.
FT   DOMAIN          191..303
FT                   /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT                   hammerhead"
FT                   /evidence="ECO:0000259|SMART:SM01008"
SQ   SEQUENCE   961 AA;  104257 MW;  851F09FA568C2723 CRC64;
     MTIEWTLNGK ALFSEVNPFK NVQEFLKEQG VLSVRDSDDH AGFTGSDTIL LDGKAINAGL
     LIAGQLDGHS VETVESLNTG NKMGYLQAAL VDAGAVQSGY NAGAAALILK ELLERVEKPT
     EEDIRDAYSG LFVRDFGYMA LFKAVELALA YMDDPEYTHG NADVEIAPEF RKDLREVGTP
     RRKVDGAQLI MGRKAFVEDR VDPEALHMKV LRSSFAHAYI TSIDVSMAKS LPGVLSIITH
     ENCPDVYYGS AGQGFPEPSP YDKRMFNRKI RHAGDRIAAV VAESEQIALD ALALIHVEYE
     ALPVVMSIDE AKAPDAPIVQ NGVIKYEAGA PDDLDAQNKD ADERDGEVIY QFPIGGEPHK
     NIASYVEGGI GDVDKGFAGS DVVLEREYES SQIQCTPLEP HSVYTKMEGD RLVIHASTQV
     PWHLRRIVAR VLGIKESNIH VIKERVGGGY GSKQDILLEE LASWVTWQTG KSVYYRYSRK
     EEFTSNSTRH VMRIKVKIGA MKDGTMTAID MTVEANTGPF GNHCLTVPMN ACSKSLPLFL
     CDHFHFDVTT YYSNIAPTGA YQGYGAPKGS YALQMAVAEL AEELGIDPLE LIEKNRVREG
     SMLEILKCLG EGREGSAARV ESCGLDGALE KGAELIEWGK KEISHDPDVK IGKGVVIIQQ
     GSGLPGLDHS NAEVKLLTDG TLLVRSGGAD LGTGLDTMCV KIASEILTVP MNEIAIVSGD
     TDSTSFDTGA YASSGTYFSG NAVVKASENL KEKILKAASE MLKEPESDLV LELPSMVKGR
     KGSVSFEDIS RDCLTGEGRG QLIGSASYTT EDSAFPYGAH FCQVAVNIKS GAIKLQKYYA
     LQDCGTPINP ELAMGQIYGG VMKSIGHTMY EEMVFDDRGR CINTDLRSYG VPMMGDVPED
     FQVHLIQTDD PFGPFGGKSI SEIAVNGAAP VIANAIHDAC GVWLRTWPLT PEKILKGLGK
     I
//