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Database: UniProt
Entry: K5BFQ5_MYCHD
LinkDB: K5BFQ5_MYCHD
Original site: K5BFQ5_MYCHD 
ID   K5BFQ5_MYCHD            Unreviewed;       765 AA.
AC   K5BFQ5;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Dimethyl sulfoxide/trimethylamine N-oxide reductase {ECO:0000313|EMBL:VCT90649.1};
DE            EC=1.7.2.3 {ECO:0000313|EMBL:VCT90649.1};
DE   SubName: Full=Molybdopterin guanine dinucleotide-containing S/N-oxide reductases family protein {ECO:0000313|EMBL:EKF24112.1};
GN   Name=dmsA {ECO:0000313|EMBL:VCT90649.1};
GN   ORFNames=C731_1872 {ECO:0000313|EMBL:EKF24112.1}, MHAS_02358
GN   {ECO:0000313|EMBL:VCT90649.1};
OS   Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 /
OS   3849) (Mycobacterium hassiacum).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1122247 {ECO:0000313|EMBL:EKF24112.1, ECO:0000313|Proteomes:UP000006265};
RN   [1] {ECO:0000313|EMBL:EKF24112.1, ECO:0000313|Proteomes:UP000006265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44199 {ECO:0000313|EMBL:EKF24112.1}, and DSM 44199 / CIP
RC   105218 / JCM 12690 / 3849 {ECO:0000313|Proteomes:UP000006265};
RX   PubMed=23209251; DOI=10.1128/JB.01880-12;
RA   Tiago I., Maranha A., Mendes V., Alarico S., Moynihan P.J., Clarke A.J.,
RA   Macedo-Ribeiro S., Pereira P.J., Empadinhas N.;
RT   "Genome sequence of Mycobacterium hassiacum DSM 44199, a rare source of
RT   heat-stable mycobacterial proteins.";
RL   J. Bacteriol. 194:7010-7011(2012).
RN   [2] {ECO:0000313|EMBL:VCT90649.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mhassiacum {ECO:0000313|EMBL:VCT90649.1};
RA   Peiro R., Begona, Cbmso G., Lopez M., Gonzalez S., Sacristan E.,
RA   Castillo E.;
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000268660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44199 / CIP 105218 / JCM 12690 / 3849
RC   {ECO:0000313|Proteomes:UP000268660};
RX   PubMed=30701245; DOI=10.1128/mra.01522-18;
RA   Sanchez M., Blesa A., Sacristan-Horcajada E., Berenguer J.;
RT   "Complete genome sequence of Mycolicibacterium hassiacum DSM 44199.";
RL   Microbiol. Resour. Announc. 8:e01522-e01522(2019).
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; AMRA01000046; EKF24112.1; -; Genomic_DNA.
DR   EMBL; LR026975; VCT90649.1; -; Genomic_DNA.
DR   RefSeq; WP_005626840.1; NZ_LR026975.1.
DR   AlphaFoldDB; K5BFQ5; -.
DR   STRING; 1122247.GCA_000379865_04775; -.
DR   KEGG; mhas:MHAS_02358; -.
DR   PATRIC; fig|1122247.3.peg.1802; -.
DR   eggNOG; COG0243; Bacteria.
DR   OrthoDB; 7376058at2; -.
DR   Proteomes; UP000006265; Unassembled WGS sequence.
DR   Proteomes; UP000268660; Chromosome 1.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0050626; F:trimethylamine-N-oxide reductase (cytochrome c) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009033; F:trimethylamine-N-oxide reductase activity; IEA:UniProtKB-EC.
DR   CDD; cd02793; MopB_CT_DMSOR-BSOR-TMAOR; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
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; IPR006658; BisC.
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   NCBIfam; TIGR00509; bisC_fam; 1.
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.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000313|EMBL:VCT90649.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006265}.
FT   DOMAIN          7..46
FT                   /note="Molybdopterin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18364"
FT   DOMAIN          50..504
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          616..730
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
FT   REGION          746..765
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   765 AA;  84311 MW;  1D83DC81AB7E9B4F CRC64;
     MAAAKTSLTH WGAFRARVAD GDIAAVAPVH TSDPSPLLGN LVGSVRHRSR VTTPAVRRGW
     LRDGPGPTDR RGADEFVPVS WDYLTELLAD ELRRVIDTHG NEAIYGGSYG WASAGRFHHA
     QSQVHRFLNC IGGYTFSRHS YSLGATGVIM PRVVGTHDNL FKRSTEWQVI VENTDLLVCF
     GGLALKNTAV NDGGTTAHPA RDALQRFRAR GGRIVSFSPL RDDVDGECEW YAPIPGTDVA
     IMLALAHVLA TEGLLDRDFL DTYCTGYDRF ERYLLGRDDG VPKSPGWAEP ICGVPADDLV
     RLARRMAAGR TLVTVSWSLQ RTRYGEQAPW MGVTLAAMLG QIGLPGGGFG HGYGSMNEPG
     LAPLRCRLPS LPQGVNPVRT FIPVAAISDM LLRPGEQFDY NGLRLTYPDI RLVYWAGGNP
     FHHHQNIPRL RRALARVDTV VVHDPYWTPM AKHADIVVPS TTAYERDDFS GSHTDPLLVA
     MPALTEPYAQ ARDDYSTFAA LAERMGVGER FTEGRTAWQW LRHLYRTWAE QLDFEVPTFD
     EFWRRGHLRL PTQTGLTLFA DFRADPQRHR LNTPSGRIEI FSADIDGFGY PDCAGHPKWY
     EPPEWLRGPR AARYPLVLLA NQPATRLHSQ LDGGATSQAS KVQGREPMRM NPKDAAVRGL
     VDGDVVRVFN DRGACLAGVV IDERVRENVV QLSTGAWYDP ADPADPDAMC VHGNPNVLTD
     DSGTSSLAHG CTGAHTLVQV EKFVGEPPPV RAHEPPVLVS EPDAR
//
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