ID A0A0D6B9M4_RHOSU Unreviewed; 819 AA.
AC A0A0D6B9M4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=trimethylamine-N-oxide reductase {ECO:0000256|ARBA:ARBA00011885};
DE EC=1.7.2.3 {ECO:0000256|ARBA:ARBA00011885};
GN Name=dmsA {ECO:0000313|EMBL:BAQ71499.1};
GN ORFNames=NHU_04386 {ECO:0000313|EMBL:BAQ71499.1};
OS Rhodovulum sulfidophilum (Rhodobacter sulfidophilus).
OG Plasmid Plasmid1 DNA {ECO:0000313|Proteomes:UP000064912}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=35806 {ECO:0000313|EMBL:BAQ71499.1, ECO:0000313|Proteomes:UP000064912};
RN [1] {ECO:0000313|EMBL:BAQ71499.1, ECO:0000313|Proteomes:UP000064912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2351 {ECO:0000313|EMBL:BAQ71499.1,
RC ECO:0000313|Proteomes:UP000064912};
RC PLASMID=Plasmid Plasmid1 DNA {ECO:0000313|Proteomes:UP000064912};
RA Nagao N.;
RT "Genome sequene of Rhodovulum sulfidophilum DSM 2351.";
RL Submitted (FEB-2015) 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 -!- 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; AP014801; BAQ71499.1; -; Genomic_DNA.
DR RefSeq; WP_060836634.1; NZ_AP014801.1.
DR AlphaFoldDB; A0A0D6B9M4; -.
DR KEGG; rsu:NHU_04386; -.
DR PATRIC; fig|35806.4.peg.4489; -.
DR eggNOG; COG0243; Bacteria.
DR Proteomes; UP000064912; Plasmid Plasmid1 DNA.
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 GO; GO:0009033; F:trimethylamine-N-oxide reductase 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 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.
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 Plasmid {ECO:0000313|EMBL:BAQ71499.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 48..88
FT /note="Molybdopterin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18364"
FT DOMAIN 92..559
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 681..793
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 819 AA; 89754 MW; C801AEFB111EDE37 CRC64;
MTSTSNSSLP LSKRSFLKGS LATGLGFAGL PLFGRGAAAQ AASKGVVSGC HWGVFYGMVE
DGRAVEFKPW EEDPAPSPQL PGVLDSLYSE SRIRYPMVRR AWLEQGPGAD PDGRGSGDFV
RVSWEKAIEL VAGEITRVRE TYGHPAVFAG SYGWKSSGKL HNCQTLLRRM LNLTGSYTNS
VGDYSTGAAQ VILPYVSGSI EVYEQCTTWD NLAGNCELMV FWGANPLNNS EISWQVADHG
SFGGVDQLKE AGVESICIDP VRTETAQHLD SEWIAPAPQT DVAMMLGIMY ALQDEGLHDQ
AFLDRYTVGF DKFLPYLLGD TDGTPKTPEW AAEICGVPAD KLRDLARRFS SKRTMLALGY
STQRQHHGEQ IHWALITLAS MLGQIGLPGG GYGLSYHYSS GGSPTHTTPI LKAVDDASGV
KVEGAAWLAA SGAVSIPVSR LVETLLNPGK VMQFNGHEVE LPEIKLAYWA GGNPFSHHQD
RNEMLRAWRR LDTFIVHDFQ WTASARHADI VLPATTSYER NDIEQVGDYA LSHIVPMKKI
VEPVFEARSD YDIFADIAAK LGKGYEFTQG LSEMDWIRGF YEAAKVEARA KSMEMPVFDA
FWDSNKPLAF PLAEAQKDFV RHADFRADPL LNALGTASGK FELYSTAIEK YGYDDCPPHA
TWMEPIERLG GPTTLYPLAV ASNHPDLRLH SQLCGTKIRE TYEVQGREPC WMHPEDAEAR
GLSDGEVVRV FNQRGQILAG LVITDVIRPG VIRVSEGGWF DPVEPRKIGS LCAYGDINNL
TTGVATSRLA QANCGQTAMA EVERFEGPLP PVTVFSQPA
//
