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
//