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Database: UniProt
Entry: A0A4P6MJF8_9RHOB
LinkDB: A0A4P6MJF8_9RHOB
Original site: A0A4P6MJF8_9RHOB 
ID   A0A4P6MJF8_9RHOB        Unreviewed;       879 AA.
AC   A0A4P6MJF8;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Trimethylamine-N-oxide reductase {ECO:0000313|EMBL:QBF31367.1};
GN   ORFNames=CFI11_09060 {ECO:0000313|EMBL:QBF31367.1};
OS   Thalassococcus sp. S3.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Thalassococcus.
OX   NCBI_TaxID=2017482 {ECO:0000313|EMBL:QBF31367.1, ECO:0000313|Proteomes:UP000289812};
RN   [1] {ECO:0000313|EMBL:QBF31367.1, ECO:0000313|Proteomes:UP000289812}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S3 {ECO:0000313|EMBL:QBF31367.1,
RC   ECO:0000313|Proteomes:UP000289812};
RA   Vejarano F., Suzuki-Minakuchi C., Ohtsubo Y., Tsuda M., Okada K.,
RA   Nojiri H.;
RT   "Complete Genome Sequence of the Marine Carbazole-Degrading Bacterium
RT   Thalassococcus sp. S3.";
RL   Submitted (JUN-2017) 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; CP022303; QBF31367.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4P6MJF8; -.
DR   KEGG; thaa:CFI11_09060; -.
DR   InParanoid; A0A4P6MJF8; -.
DR   OrthoDB; 9759518at2; -.
DR   Proteomes; UP000289812; Chromosome.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 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; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   InterPro; IPR006311; TAT_signal.
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; PF01568; Molydop_binding; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000289812};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..879
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5020619984"
FT   DOMAIN          84..542
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          654..769
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   879 AA;  98169 MW;  35A5EA0356D1175D CRC64;
     MTLSRRSFLK SSSSIVMAAA VPQMAWASAG RDVTFVPHAG QAGAFWGMLE EGKLVRAIPR
     TEFDPRPTKM VSEGIVSRTY HKTRVLYPHV RRSYLEGYES GDVKPELRAR DEFVRVDWDT
     ALGLVSRAIL DTIDAHGNEG IFSTSYGAWA HGGVLTPNVL QGRFFNLIGG ASVTVGDYSG
     GAGQIIMPHV LGDMEVYSRQ TSWWQVLQHC ETFVLIGTDP HNNGRAEGGT TDHSMFPRWE
     VIKEAGVKFI SINPQRTTTD EWLRAQWLKI IPNTDTALFL AMSNHVYRKG TYDKDFLETY
     TVGWERFIDY LEGKDDGVPK TPEWAAKITG INAKRIRALA DRCARTRTQF AGSWAIQRAQ
     HGEMPYWAIT AFAAMTGQIG LPGGGVGFSW HWGQGGALFA QARAPGGLPQ GRNRVVGICP
     ASRLNEMLLN PGKEFTRNGG TFKFPDVHMI YNSGNNFASH QQDTNELLRA MEKVHTVVCQ
     DPWWTASARF ADIVLPATST VERDDISSGG TYSKDKVYAM RQVIDPLGES LDDFEIFRRL
     AEMFGVEGQF TDNRERREII EESYFKSTAA EYMDFDAFWD GGVARVPQPP EEIEWVRHGD
     FRTDPEANPL ATPSGKVEIY SEAIAKMNIP DCPPMPMWLE PDEYLGNAEP DEVHVVSPHP
     YNRIHSQFAQ SDLRHEMNIK DREFLLINPD DAAEREIEDG DLVELYNDRG AVIVGARVSD
     DIMKGVVSMY EGAWLSFDSK GRCNSGAINI LTSSRRSSGL SQATTANTCL ARMRKATDVD
     GPNMAYEPPA IAPEPVKLDV SAFNLERAYD LQETFTAEME PGEKLFYEKC TLCHVPQDPA
     AHTMRQWESI TASMFPNAGV TPEEEEQILT FLAKYAKPE
//
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