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Database: UniProt
Entry: F5XKR8_MICPN
LinkDB: F5XKR8_MICPN
Original site: F5XKR8_MICPN 
ID   F5XKR8_MICPN            Unreviewed;       723 AA.
AC   F5XKR8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Putative biotin sulfoxide reductase {ECO:0000313|EMBL:BAK36140.1};
GN   Name=bisC {ECO:0000313|EMBL:BAK36140.1};
GN   OrderedLocusNames=MLP_31260 {ECO:0000313|EMBL:BAK36140.1};
OS   Microlunatus phosphovorus (strain ATCC 700054 / DSM 10555 / JCM 9379 / NBRC
OS   101784 / NCIMB 13414 / VKM Ac-1990 / NM-1).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Microlunatus.
OX   NCBI_TaxID=1032480 {ECO:0000313|EMBL:BAK36140.1, ECO:0000313|Proteomes:UP000007947};
RN   [1] {ECO:0000313|EMBL:BAK36140.1, ECO:0000313|Proteomes:UP000007947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700054 / DSM 10555 / JCM 9379 / NBRC 101784 / NCIMB 13414
RC   / VKM Ac-1990 / NM-1 {ECO:0000313|Proteomes:UP000007947};
RA   Hosoyama A., Sasaki K., Harada T., Igarashi R., Kawakoshi A., Sasagawa M.,
RA   Fukada J., Nakamura S., Katano Y., Hanada S., Kamagata Y., Nakamura N.,
RA   Yamazaki S., Fujita N.;
RT   "Whole genome sequence of Microlunatus phosphovorus NM-1.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR   EMBL; AP012204; BAK36140.1; -; Genomic_DNA.
DR   RefSeq; WP_013864004.1; NC_015635.1.
DR   AlphaFoldDB; F5XKR8; -.
DR   STRING; 1032480.MLP_31260; -.
DR   KEGG; mph:MLP_31260; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_13_3_11; -.
DR   OrthoDB; 9759518at2; -.
DR   Proteomes; UP000007947; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd02793; MopB_CT_DMSOR-BSOR-TMAOR; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 2.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   Gene3D; 3.90.55.10; Dimethylsulfoxide Reductase, domain 3; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR041954; CT_DMSOR/BSOR/TMAOR.
DR   InterPro; IPR041460; Molybdopterin_N.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR   PANTHER; PTHR43742:SF10; TRIMETHYLAMINE-N-OXIDE REDUCTASE 2; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF18364; Molybdopterin_N; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR   PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007947}.
FT   DOMAIN          8..48
FT                   /note="Molybdopterin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18364"
FT   DOMAIN          52..459
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          574..692
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   723 AA;  78071 MW;  E07A136100CFFB54 CRC64;
     MSPRRPIHSA HWGAYRPRVE AGRLIGAEPF EADPDPSPLL TSIPGVVHAT NRVTRPAVRK
     TWLEGRPGRR GADPFVEIDW DEALDLVADT LRRVYRESGP AAIFGGSYGW SSAGRLHHAK
     TQLKHFLACT GGYTGQVSNY SYGAADGILP HVLGDARMVE KHASTWTELA EHTDTLLMFG
     GFPAKNVQLE SGGVGAHSAR LGLESVLASG TQLINVNPVR SDAPEHSAVS WLPIRPNTDT
     ALILAVIGRL VETIESLVQR ISHGRTLITG TWALQRADHG EQPYWAIIAL AAALGQIGLP
     GGGFGFGYGS TGGVGSVARS FGTPAFQARP NPIDSDVPAA RLTDMLLHPG EGYEFNGASY
     TYPKIDLIYW AGGNPFHHHQ DLNRLAEAWQ RPGTVVVHDS WWTPTARMAD IVLPATTTLE
     RDDIAAGSKE RFVVAMKRSI DPQGQARNDR VILADLAKRL GVWQEYTDGR DDAEALRWMY
     DKARSSAAEH GCAMPDFDTF WAAGFFEFPV GESIPPFAEF RHDPVSHPLS TPSGRIEIFS
     ETIASFGYDD CPGHPSWLEP YEWLGSTAPA TVLLHLLSPQ PATRLHSQLD MGAVSIDSKI
     AGREPCTMNL RDAEIRGIQD GDLIRVWNER GELYAGARLS ADVMPGVALL ATGAWYTPAD
     PSVPGSPELH GNPNVLARDV GTSRLAQGAT AQSLLVRIEK AGPDVPWVDP HGVPAGVTAG
     VGE
//
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