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
//