ID D4F7F2_EDWTA Unreviewed; 830 AA.
AC D4F7F2;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=trimethylamine-N-oxide reductase {ECO:0000256|ARBA:ARBA00011885};
DE EC=1.7.2.3 {ECO:0000256|ARBA:ARBA00011885};
GN ORFNames=EDWATA_02687 {ECO:0000313|EMBL:EFE22315.1};
OS Edwardsiella tarda ATCC 23685.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=500638 {ECO:0000313|EMBL:EFE22315.1, ECO:0000313|Proteomes:UP000003692};
RN [1] {ECO:0000313|EMBL:EFE22315.1, ECO:0000313|Proteomes:UP000003692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23685 {ECO:0000313|EMBL:EFE22315.1,
RC ECO:0000313|Proteomes:UP000003692};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2010) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFE22315.1}.
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DR EMBL; ADGK01000232; EFE22315.1; -; Genomic_DNA.
DR RefSeq; WP_005287899.1; NZ_GG739633.1.
DR AlphaFoldDB; D4F7F2; -.
DR HOGENOM; CLU_000422_13_3_6; -.
DR Proteomes; UP000003692; Unassembled WGS sequence.
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 Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 64..104
FT /note="Molybdopterin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18364"
FT DOMAIN 108..568
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 687..802
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 830 AA; 91013 MW; 69C184D7FC058A38 CRC64;
MNKKTAPTAA PLRISRRHFL AGGAALLGAP LLAGLWPKSA LAQAISLALP QFTALQPAQK
GPLTGAHWGA FEAIVSDDRM VGVRAVSDDP YPNELITMAP YQVHAANRIK YPMVRKHYLE
GGPQNGHPEL RGCDEWVRVS WDQALTLVSD QITRLQRQYG PQSIHAGSYG WKSVGMLHNS
RTLLQRLMNL SGGFLGYAGD YSTGAAQVIM THVVGSMEVY EQQTAWPNVI EHSELVVLWG
CNPMITLENS WNMPDHVGQT GFEALKKKGT RIISIDPVRS ASTTQLNAEW IAPHPYTDAA
MLLGIAHTLM SEKLHDRDFL TTYTVGFDRF ADYLNGKDDG VVKDAAWAAA ISGVEAETLR
QLARDMARQR TMIMAGWGIQ RQHHGEQPHW LLVTVAAMLG QIGLPGGGFG FSYHYSSGGS
PTARGGILSG ISAGNAPKNS PTPIPVARIA DCLANPGKTI DFNGGKVTYP DVKMVYVAGG
NPFGHHQNTN NLIEAWRRPE TIVVNEPYWT ATAKYADIVL PATTSYERND LEMGGDYSQL
YVFPMHQCVP PQHEARNDFA IFAGLAEKLG VLEAFTEGKD EQQWLKGMYD GMAAQARNAR
VALPPFDMFW ASNNYIRFPI PPANKEWVRY ADFRANPLLN PLGTPSGKIE IYSDTIAAMN
YPDCKGLPSW MPPYEWYQSE VAQRFPLSLS TAHAVNRLHS QLDNTPLREK YAVANREAIL
IHPQDAKARG IADGDLVRAW NDRGQILVGA IVTQDIRPGV VRISEGAWFD PADPAKPGSL
CRNGNVNCLT FDIGSSRLAQ GNCGHMAQLE IEKFQGTPPA NTAHDVPRGA
//
