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Database: UniProt
Entry: Q2RUV7_RHORT
LinkDB: Q2RUV7_RHORT
Original site: Q2RUV7_RHORT 
ID   Q2RUV7_RHORT            Unreviewed;       823 AA.
AC   Q2RUV7;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   24-JAN-2024, entry version 116.
DE   RecName: Full=trimethylamine-N-oxide reductase {ECO:0000256|ARBA:ARBA00011885};
DE            EC=1.7.2.3 {ECO:0000256|ARBA:ARBA00011885};
GN   OrderedLocusNames=Rru_A1287 {ECO:0000313|EMBL:ABC22088.1};
OS   Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS   NCIMB 8255 / S1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=269796 {ECO:0000313|EMBL:ABC22088.1, ECO:0000313|Proteomes:UP000001929};
RN   [1] {ECO:0000313|EMBL:ABC22088.1, ECO:0000313|Proteomes:UP000001929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1
RC   {ECO:0000313|Proteomes:UP000001929};
RX   PubMed=21886856; DOI=10.4056/sigs.1804360;
RA   Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA   Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA   Mavromatis K., Richardson P., Rohde M., Goker M., Klenk H.P., Zhang Y.,
RA   Roberts G.P., Reslewic S., Schwartz D.C.;
RT   "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL   Stand. Genomic Sci. 4:293-302(2011).
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR   EMBL; CP000230; ABC22088.1; -; Genomic_DNA.
DR   RefSeq; WP_011389042.1; NC_007643.1.
DR   RefSeq; YP_426375.1; NC_007643.1.
DR   AlphaFoldDB; Q2RUV7; -.
DR   STRING; 269796.Rru_A1287; -.
DR   EnsemblBacteria; ABC22088; ABC22088; Rru_A1287.
DR   KEGG; rru:Rru_A1287; -.
DR   PATRIC; fig|269796.9.peg.1353; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_13_3_5; -.
DR   OMA; KPWVRHA; -.
DR   PhylomeDB; Q2RUV7; -.
DR   Proteomes; UP000001929; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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   CDD; cd02793; MopB_CT_DMSOR-BSOR-TMAOR; 1.
DR   CDD; cd02769; MopB_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   InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   NCBIfam; TIGR00509; bisC_fam; 1.
DR   NCBIfam; TIGR01409; TAT_signal_seq; 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.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR   PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 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   ECO:0000313|EMBL:ABC22088.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001929};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..43
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           44..823
FT                   /note="trimethylamine-N-oxide reductase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004215040"
FT   DOMAIN          51..91
FT                   /note="Molybdopterin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18364"
FT   DOMAIN          95..562
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          680..798
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   823 AA;  89341 MW;  704AF00E0C84E255 CRC64;
     MSKMSPPTAF AAQTRRTFLK ASAAAGALGL VAPSLLSAGV ARAAEDGEVL TGSHWGAFRA
     TVKGGKMTAI KPWEKDPHPS HQLTGVMDSI YSPTRIKYPM VRRAFLEKGP GASPETRGAG
     DFVRVTWDQA LDLVAKELTR VRKDHGPTSI FAGSYGWMSP GKLHNCRSLV RRLLNQTGGF
     VSSSGDYSTG ASQVIMPHVM GTLEVYEQPT VWPVVVEHSD LVVFWGADPM TTNQIGWLIP
     DHGAYVGLKA LKESGKKVIC IDPVRTETCD YLGAEWIAPK PQTDMAMMLG VAHTLYTEKL
     HDQSFLDDYT FGFDRFLPYL TGESDKTPKS AEWASAICGI PAEVIKDLAR RIVKGRTMLA
     SGWSMQRQHH GEQIHWMLVT LASMVGQIGL PGGGFGLSYH YANGGSPSAT GPVLPAISDG
     SAAVKGAAWL AAGGAASIPV ARVVDMLMNP GKEFDFNGTK AIYPDTKLIY WTGGNPFAHH
     QNRNRMVEAF RKVETFIVHD FQWTATARHA DIVLPATTSY ERNDIEQIGD YALSSVLAMK
     KVVEPVFEAR SDFDILAAVA ERLGTRDAFT EGKDEMGWIK EFYDNALGQA KAKGVTMPDF
     ETFWKGEGVV SFPISDEAKA FVRYSAFRED PLLEPLGTPT GKIEIYSKNI EKMGYDDCPA
     HPTWMEPVER LDGPGAKFPL HITTSHPKSR LHSQLCGTKL RDSYTVAGRE PCLINEADAK
     ARGISNGDVV RVFNDRGQIL AGAVVTNAIR PGVIRVNEGG WYDPTEPTKP GSLCKYGDVN
     VLTVDIGTSK LAQGNCGHTA IGDVEKYAEA APAVTVFAAP KNA
//
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