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UniProtKB/Swiss-Prot entry P46923

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TORZ_ECOLI
Primary accession number P46923
Secondary accession numbers P76292 P97187
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on November 1, 1997 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 71)
Name and origin of the protein
Protein name Trimethylamine-N-oxide reductase 2 [Precursor]
Synonyms TMAO reductase 2
Trimethylamine oxidase 2
EC 1.7.2.3
Gene name
Name: torZ
Synonyms: bisZ
OrderedLocusNames: b1872, JW1861
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / ACC5;
DOI=10.1007/BF02198832; PubMed=8919859 [NCBI, ExPASy, EBI, Israel, Japan]
del Campillo-Campbell A., Campbell A.M.;
"Alternative gene for biotin sulfoxide reduction in Escherichia coli K-12.";
J. Mol. Evol. 42:85-90(1996).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/3.6.379; PubMed=9097040 [NCBI, ExPASy, EBI, Israel, Japan]
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.;
"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map.";
DNA Res. 3:379-392(1996).
[3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
 CHARACTERIZATION, AND PROTEIN SEQUENCE OF 32-39.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
DOI=10.1128/JB.182.20.5779-5786.2000; PubMed=11004177 [NCBI, ExPASy, EBI, Israel, Japan]
Gon S., Patte J.-C., Mejean V., Iobbi-Nivol C.;
"The torYZ (yecK bisZ) operon encodes a third respiratory trimethylamine N-oxide reductase in Escherichia coli.";
J. Bacteriol. 182:5779-5786(2000).
Comments
  • FUNCTION: Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an anaerobic reaction coupled to energy-yielding reactions. Can also reduce other N- and S-oxide compounds such as 4-methylmorpholine-N-oxide and biotin sulfoxide (BSO), but with a lower catalytic efficiency.
  • CATALYTIC ACTIVITY: Trimethylamine + 2 (ferricytochrome c)-subunit + H2O = trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H+.
  • COFACTOR: Molybdenum (molybdopterin) (By similarity).
  • SUBCELLULAR LOCATION: Periplasm.
  • PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
  • MISCELLANEOUS: Expression of torYZ allows E.coli to grow anaerobically on a wider range of substrates than does expression of torCAD.
  • SIMILARITY: Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.
  • CAUTION: Was originally (PubMed:8919859) thought to be a biotin sulfoxide reductase.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U38839; AAC44131.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC74942.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA15682.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR H64949; H64949.
RefSeq AP_002492.1; -.
NP_416386.4; -.
3D structure databases
HSSP Q52675; 1DMS. [HSSP ENTRY / PDB]
ModBase P46923.
Protein-protein interaction databases
IntAct P46923; -.
Enzyme and pathway databases
BioCyc EcoCyc:G7022-MON; -.
Organism-specific databases
EchoBASE EB3061; -.
EcoGene EG13276; torZ.
Ontologies
GO
GO:0050626; Molecular function: trimethylamine-N-oxide reductase (cytochrome c) activity (inferred from electronic annotation from EC).
QuickGo view.
Family and domain databases
InterPro IPR009010; Asp_de-COase-like_fold.
IPR006658; BisC.
IPR006656; Mopterin_OxRdtase.
IPR006655; Mopterin_OxRdtase_prok_CS.
IPR006657; MPT_dinuc_bd.
IPR006311; Tat.
Graphical view of domain structure.
Gene3D G3DSA:2.40.40.20; Asp_decarboxylase-like_fold; 1.
Pfam PF00384; Molybdopterin; 1.
PF01568; Molydop_binding; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00509; bisC_fam; 1.
TIGR01409; TAT_signal_seq; 1.
PROSITE PS00551; MOLYBDOPTERIN_PROK_1; FALSE_NEG.
PS00490; MOLYBDOPTERIN_PROK_2; 1.
PS00932; MOLYBDOPTERIN_PROK_3; 1.
PS51318; TAT; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P46923.
Genome annotation databases
GeneID 946389; -.
GenomeReviews U00096_GR; b1872.
AP009048_GR; JW1861.
KEGG ecj:JW1861; -.
eco:b1872; -.
Phylogenomic databases
HOGENOM P46923; -.
Genome annotation databases
CMR P46923; b1872.
Other
ProtoNet P46923.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; Molybdenum; Oxidoreductase; Periplasm; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    31  31     Tat-type signal. 
CHAIN   32   809  778     Trimethylamine-N-oxide reductase 2. PRO_0000019163
CONFLICT   76    76        A -> T (in Ref. 1; AAC44131). 
CONFLICT   291   292        HD -> TI (in Ref. 1; AAC44131). 
CONFLICT   299   304        YTTGYP -> TLPGIR (in Ref. 1; AAC44131). 
CONFLICT   406   409        EMSA -> DFSGP (in Ref. 1; AAC44131). 
CONFLICT   801   803        AFD -> GFG (in Ref. 1; AAC44131). 
Sequence information
Length: 809 AA [This is the length of the unprocessed precursor] Molecular weight: 88964 Da [This is the MW of the unprocessed precursor] CRC64: 44A84F6302531D09 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTLTRREFIK HSGIAAGALV VTSAAPLPAW AEEKGGKILT AGRWGAMNVE VKDGKIVSST 

        70         80         90        100        110        120 
GALAKTIPNS LQSTAADQVH TTARIQHPMV RKSYLDNPLQ PAKGRGEDTY VQVSWEQALK 

       130        140        150        160        170        180 
LIHEQHDRIR KANGPSAIFA GSYGWRSSGV LHKAQTLLQR YMNLAGGYSG HSGDYSTGAA 

       190        200        210        220        230        240 
QVIMPHVVGS VEVYEQQTSW PLILENSQVV VLWGMNPLNT LKIAWSSTDE QGLEYFHQLK 

       250        260        270        280        290        300 
KSGKPVIAID PIRSETIEFF DDNATWIAPN MGTDVALMLG IAHTLMTQGK HDKVFLEKYT 

       310        320        330        340        350        360 
TGYPQFEEYL TGKSDNTPKS AVWAAEITGV PEAQIVKLAE LMAANRTMLM AGWGIQRQQY 

       370        380        390        400        410        420 
GEQKHWMLVT LAAMLGQIGT PGGGFGFSYH YSNGGNPTRV GGVLPEMSAA IAGHASEAAD 

       430        440        450        460        470        480 
DGGMTAIPVA RIVDALENPG GKYQHNGKEQ TYPNIKMIWW AGGGNFTHHQ DTNRLIKAWQ 

       490        500        510        520        530        540 
KPEMIVVSEC YWTAAAKHAD IVLPITTSFE RNDLTMTGDY SNQHIVPMKQ AVAPQFEARN 

       550        560        570        580        590        600 
DFDVFADLAE LLKPGGKEIY TEGKDEMAWL KFFYDAAQKG ARAQRVTMPM FNAFWQQNKL 

       610        620        630        640        650        660 
IEMRHSEKNE QYVRYGDFRA DPVKNALGTP SGKIEIYSKT LEKFGYKDCP AHPTWLAPDE 

       670        680        690        700        710        720 
WKGTADEKQL QLLTAHPAHR LHSQLNYAEL RKKYAIADRE PITIHTEDAA RFGIANGDLV 

       730        740        750        760        770        780 
RVWNKRGQIL TGAVVTDGIK KGVVCVHEGA WPDLENGLCK NGSANVLTAD IPSSQLANAC 

       790        800 
AGNSALVYIE KYTGNAPKLT AFDQPAVQA
P46923 in FASTA format

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