ID   B7USP9_ECO27            Unreviewed;       809 AA.
AC   B7USP9;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   02-SEP-2026, entry version 88.
DE   RecName: Full=trimethylamine-N-oxide reductase {ECO:0000256|ARBA:ARBA00011885};
DE            EC=1.7.2.3 {ECO:0000256|ARBA:ARBA00011885};
GN   Name=torZ {ECO:0000313|EMBL:CAS09545.1};
GN   OrderedLocusNames=E2348C_1997 {ECO:0000313|EMBL:CAS09545.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS09545.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS09545.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA   Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA   Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|PIRSR:PIRSR606658-1};
CC       Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC       bis-MGD) cofactor per subunit. {ECO:0000256|PIRSR:PIRSR606658-1};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC       {ECO:0000256|PROSITE-ProRule:PRU00648}.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR   EMBL; FM180568; CAS09545.1; -; Genomic_DNA.
DR   RefSeq; WP_000176870.1; NC_011601.1.
DR   AlphaFoldDB; B7USP9; -.
DR   KEGG; ecg:E2348C_1997; -.
DR   HOGENOM; CLU_000422_13_3_6; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter.
DR   GO; GO:0009055; F:electron transfer activity; IEA:TreeGrafter.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:TreeGrafter.
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:0009061; P:anaerobic respiration; IEA:TreeGrafter.
DR   CDD; cd02793; MopB_CT_DMSOR-BSOR-TMAOR; 1.
DR   CDD; cd02769; MopB_DMSOR-BSOR-TMAOR; 1.
DR   FunFam; 2.40.40.20:FF:000009; Biotin sulfoxide reductase 2; 1.
DR   FunFam; 3.40.228.10:FF:000003; Biotin sulfoxide reductase 2; 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; IPR050612; Prok_Mopterin_Oxidored.
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   ECO:0000256|PIRSR:PIRSR606658-1};
KW   Molybdenum {ECO:0000256|ARBA:ARBA00022505, ECO:0000256|PIRSR:PIRSR606658-
KW   1}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008205};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|PROSITE-
KW   ProRule:PRU00648}.
FT   CHAIN           32..809
FT                   /note="trimethylamine-N-oxide reductase"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00648"
FT                   /id="PRO_5049024797"
FT   DOMAIN          40..80
FT                   /note="Molybdopterin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18364"
FT   DOMAIN          84..550
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          670..779
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
FT   BINDING         145
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606658-1"
FT   BINDING         357
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606658-1"
FT   BINDING         468
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606658-1"
FT   BINDING         511
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606658-1"
FT   BINDING         541
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606658-1"
FT   BINDING         765
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606658-1"
SQ   SEQUENCE   809 AA;  88874 MW;  B82DFC1D3D26C5CA CRC64;
     MTLTRREFIK HSGIAAGTLV VTSAAPLPAW AEEKGGKILT AGRWGAMNVE VKDGKIVSST
     GALAKTIPNS LQSTAADQVH TTARIQHPMV RKSYLDNPLQ PAKGRGEDTY VQVSWEQALK
     LIHEQHDRIR KANGPSAIFA GSYGWRSSGV LHKAQTLLQR YMNLAGGYSG HSGDYSTGAA
     QVIMPHVVGS VEVYEQQTSW PLILENSQVV VLWGMNPLNT LKIAWSSTDE QGLEYFHQLK
     KSGKPVIAID PIRSETIEFF GDNATWIAPN MGTDVALMLG IAHTLMTQGK HDKVFLEKYT
     TGYPQFEEYL TGKSDNTPKS AAWAAEITGV PEAQIVKLAE LMAANRTMLM AGWGIQRQQY
     GEQKHWMLVT LAAMLGQIGT PGGGFGFSYH YSNGGNPTRV GGVLPEMSAA IAGQASEAAD
     DGGMTAIPVA RIVDALENPG GKYQHNGKEQ TYPNIKMIWW AGGGNFTHHQ DTNRLIKARQ
     KPEMIVVSEC YWTAAAKHAD IVLPITTSFE RNDLTMTGDY SNQHIVPMKQ AVAAQFEARN
     DFDVFADLAE LLKPGGKEIY TEGKDEMAWL KFFYDAAQKG ARAQRVTMPM FNAFWQQNKL
     IEMRRSEKNE QYIRYGDFRA DPVKNALGTP SGKIEIYSRT LEKFGYKDCP AHPTRLAPDE
     WKGTADEKQL QLLTAHPAHR LHSQLNYAEL RKKYAVADRE PITIHTEDAA RFGIANGDLV
     RVWNKRGQIL TGAVVTDGIK KGVVCVHEGA WPDLENGLCK NGSANVLTAD IPSSQLANAC
     AGNSALVYIE KYTGNAPKLT AFDQPAIQA
//