TORA_SHEON
ID TORA_SHEON Reviewed; 829 AA.
AC Q8EHI9;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Trimethylamine-N-oxide reductase;
DE Short=TMAO reductase;
DE Short=Trimethylamine oxidase;
DE EC=1.7.2.3;
DE Flags: Precursor;
GN Name=torA; OrderedLocusNames=SO_1232;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
CC -!- FUNCTION: Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an
CC anaerobic reaction coupled to energy-yielding reactions. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(III)-[cytochrome c] + H2O + trimethylamine = 2 Fe(II)-
CC [cytochrome c] + 3 H(+) + trimethylamine N-oxide;
CC Xref=Rhea:RHEA:24236, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15724,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:58389; EC=1.7.2.3;
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AE014299; AAN54300.1; -; Genomic_DNA.
DR RefSeq; NP_716855.1; NC_004347.2.
DR RefSeq; WP_011071460.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EHI9; -.
DR SMR; Q8EHI9; -.
DR STRING; 211586.SO_1232; -.
DR PaxDb; Q8EHI9; -.
DR KEGG; son:SO_1232; -.
DR PATRIC; fig|211586.12.peg.1183; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_6; -.
DR OMA; KPWVRHA; -.
DR OrthoDB; 88184at2; -.
DR PhylomeDB; Q8EHI9; -.
DR BioCyc; SONE211586:G1GMP-1142-MON; -.
DR BRENDA; 1.7.2.3; 5706.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0030151; F:molybdenum ion binding; IBA:GO_Central.
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; IBA:GO_Central.
DR CDD; cd02793; MopB_CT_DMSOR-BSOR-TMAOR; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
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; IPR011887; TorA.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF18364; Molybdopterin_N; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR TIGRFAMs; TIGR02164; torA; 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; Molybdenum; Oxidoreductase; Periplasm; Reference proteome;
KW Signal.
FT SIGNAL 1..31
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 32..829
FT /note="Trimethylamine-N-oxide reductase"
FT /id="PRO_0000019158"
FT BINDING 180
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250"
SQ SEQUENCE 829 AA; 92594 MW; 9F065DFE90E05808 CRC64;
MNRRDFLKGL ASTSFVALGG SSVLAPLNAL ANTGLNENEW LTTGSHFGAF KIKRKNGMIA
EVKAFDLDKY PTDMINGIRG MVYNPSRVRY PMVRLDFLLK GHKSNTQQRG DFRFVRVTWD
KALKLFKHSL DEVQTKYGPS GLHAGQTGWR ATGQLHSSTS HMQRAVGMHG NFVKKIGDYS
TGAGQTILPY VLGSTEVYAQ GTSWPLILEN SNTIVLWSND PYKNLQVGWN AETHEAFAYL
AQLKEKVKQG KIRVISIDPV VTKTQAYLGC EQLYVNPQTD VTLMLAIAHE MITQKLHDEK
FIQGYSLGFE EFVPYVMGTK DGIAKTPEWA APICGVEPHI IRDLAKTLVK GRTQIMMGWC
IQRQQHGEQP YWMAAVLATM IGQIGLPGGG ISYGHHYSSI GVPATTAAAP GAFPRNLDEN
QKPLFDSTDF KGASSTIPVA RWIDAILEPG KTIDANGSKV VYPDIKMMIF SGNNPWNHHQ
DRNRMKQAFQ KLECVVSIDV NWTATCRFSD IVLPACTTYE RNDIDVYGAY ANRGILAMQK
MVEPLFESLS DFEIFTRFAA LLGKEKEYTR NMSEMEWIET LYNECKAANA GKYEMPDFAT
FWKQGYVHFG EGELWTRHAD FRNDPEINPL GTPSGLIEIF SRKIEQFGYD DCQGHPMWME
KAERSHGGPG SNKYPMWLQS CHPDHRLHSQ MCESKEYRET YTVNGREPVY ISPEDAKTRG
IKDGDIVRVF NDRGQLLAGA VVSDRFPKGV VRIHEGAWYG PVGKDGSVEG GAEIGALCSY
GDPNTLTLDI GTSKLAQACS AYTCLVEFEK YQGKAPKVSS FDGPIEVEI
