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Database: UniProt
Entry: A0A2A8S9B6_9BACI
LinkDB: A0A2A8S9B6_9BACI
Original site: A0A2A8S9B6_9BACI 
ID   A0A2A8S9B6_9BACI        Unreviewed;       751 AA.
AC   A0A2A8S9B6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Xanthine dehydrogenase subunit D {ECO:0000313|EMBL:PEZ05076.1};
GN   Name=pucD {ECO:0000313|EMBL:PEZ05076.1};
GN   ORFNames=CN326_15135 {ECO:0000313|EMBL:PEZ05076.1};
OS   Bacillus sp. AFS018417.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2033491 {ECO:0000313|EMBL:PEZ05076.1, ECO:0000313|Proteomes:UP000220085};
RN   [1] {ECO:0000313|EMBL:PEZ05076.1, ECO:0000313|Proteomes:UP000220085}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AFS018417 {ECO:0000313|EMBL:PEZ05076.1,
RC   ECO:0000313|Proteomes:UP000220085};
RG   Agbiome Team Llc;
RA   Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA   Shank E.A., Bowers A.;
RT   "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT   roles of natural products in bacterial physiology.";
RL   Submitted (SEP-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:PEZ05076.1}.
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DR   EMBL; NTTM01000036; PEZ05076.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A8S9B6; -.
DR   OrthoDB; 9759099at2; -.
DR   Proteomes; UP000220085; Unassembled WGS sequence.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1.
DR   Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 4.
DR   InterPro; 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; IPR017609; Xanthine_dehydrogenase_dsu.
DR   NCBIfam; TIGR03196; pucD; 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; PF02738; MoCoBD_1; 1.
DR   Pfam; PF20256; MoCoBD_2; 1.
DR   SMART; SM01008; Ald_Xan_dh_C; 1.
DR   SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR   SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000220085}.
FT   DOMAIN          23..129
FT                   /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT                   hammerhead"
FT                   /evidence="ECO:0000259|SMART:SM01008"
SQ   SEQUENCE   751 AA;  81793 MW;  C2FE0AB6C3DCF3D2 CRC64;
     MHLNRESSGE NWRVRPDGVE KVTGTLKYLT DLTFPTMLFG KIMRSHYPHA RIIAIHTEKA
     KKLKGVHGVL TYKDIPGLNG FGILDPDQPV LCHDKVRFIG DAVAAVAAES KEIAEQALKL
     IEVEYEVFPV VDDPELSLLP SAPQIHEKGN ILHRSSFKKG DLDEGFKNCE FIIEETYDTP
     RQIHAYMETE GGVVVPDKDG GIIVYMGTQH GYCDRFQLSR ILNLDETKIR VVSSPMGGSF
     GGKDELNVQS YGALLALHTG YPVKIHQNRR ESIQSGIKRH PMRIKMKTGV DRDGNILAHE
     ATIIADTGAY ATLGLAVLEC AVENTVGPYL IPNINIDGVS VYTNNGVSGE FRGFGSNQVV
     FALEGQLDRL AEKLKMDPIE LREKNIKRLD GLGALDQTIA PTDGAKEVLD AIKQSNILRM
     KKTDNGKWKR RGAGIAITIL GQGLGHGIPD PGAGCMSISK DGKIEAAFGV EEVGQGVLAV
     IETLLMKAFK CGSDDLNIVI GDTEKVPHSG STTASRATTM IWLAIEKMRE SFESQILQRA
     SQMTGLPKQQ LCLGPGGIWR ESKLIVSYVN LAGQLNEPIE VSVEFPYPQS NDTVQKGRYL
     YSFAAVAAEV EVDLLTGKVT VLGLDQAIAA GPVVSPMGYL GQIEGSGVMS IGYTLTEDCP
     MEKGKYVTEN FDTYLIPTIC DVPPDMNVYA IETVQSGDTF GPKGIGEIGT VAVAPAIAKA
     IHDAIGYWCN RIPVSREEIL QAVEKEGRIW T
//
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