Reviewed, UniProtKB/Swiss-Prot P46923 (TORZ_ECOLI)

Names and origin

Protein names

Recommended name:
    Trimethylamine-N-oxide reductase 2
      Short name=TMAO reductase 2
      Short name=Trimethylamine oxidase 2
    EC=1.7.2.3

Gene names

Name:	torZ
Synonyms:	bisZ
Ordered Locus Names:	b1872, JW1861

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	809 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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 + H(2)O = trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H(+).
Cofactor	Molybdenum (molybdopterin) By similarity.
Subcellular location	Periplasm.
Post-translational modification	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.
Sequence similarities	Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.
Caution	Was originally (Ref.1) thought to be a biotin sulfoxide reductase.

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Ligand	Molybdenum
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro molybdenum ion binding Inferred from electronic annotation. Source: InterPro trimethylamine-N-oxide reductase (cytochrome c) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 31	31	Tat-type signal
	Chain	32 – 809	778	Trimethylamine-N-oxide reductase 2		PRO_0000019163
Experimental info
	Sequence conflict	76	1	A → T in AAC44131. Ref.1
	Sequence conflict	291 – 292	2	HD → TI in AAC44131. Ref.1
	Sequence conflict	299 – 304	6	YTTGYP → TLPGIR in AAC44131. Ref.1
	Sequence conflict	406 – 409	4	EMSA → DFSGP in AAC44131. Ref.1
	Sequence conflict	801 – 803	3	AFD → GFG in AAC44131. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P46923-1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 44A84F6302531D09	FASTA	809	88,964
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Alternative gene for biotin sulfoxide reduction in Escherichia coli K-12." del Campillo-Campbell A., Campbell A.M. J. Mol. Evol. 42:85-90(1996) [PubMed: 8919859] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / ACC5.
[2]	"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." 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. DNA Res. 3:379-392(1996) [PubMed: 9097040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." 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. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"The torYZ (yecK bisZ) operon encodes a third respiratory trimethylamine N-oxide reductase in Escherichia coli." Gon S., Patte J.-C., Mejean V., Iobbi-Nivol C. J. Bacteriol. 182:5779-5786(2000) [PubMed: 11004177] [Abstract] Cited for: CHARACTERIZATION, PROTEIN SEQUENCE OF 32-39. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U38839 Genomic DNA. Translation: AAC44131.1. U00096 Genomic DNA. Translation: AAC74942.1. Different initiation. AP009048 Genomic DNA. Translation: BAA15682.1.
PIR	H64949.
RefSeq	AP_002492.1. NP_416386.4.
3D structure databases
HSSP	HSSP built from PDB template 1DMS based on UniProtKB Q52675.
ModBase	Search...
Genome annotation databases
GeneID	946389.
GenomeReviews	Gene locus b1872 in contig U00096_GR. Gene locus JW1861 in contig AP009048_GR.
KEGG	ecj:JW1861. eco:b1872.
Organism-specific databases
EchoBASE	EB3061.
EcoGene	EG13276. torZ.
CMR	Search...
Phylogenomic databases
HOGENOM	P46923.
Enzyme and pathway databases
BioCyc	EcoCyc:G7022-MON. MetaCyc:G7022-MON.
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]
Gene3D	G3DSA:2.40.40.20. Asp_decarboxylase-like_fold. 1 hit.
Pfam	PF00384. Molybdopterin. 1 hit. PF01568. Molydop_binding. 1 hit. [Graphical view]
TIGRFAMs	TIGR00509. bisC_fam. 1 hit. TIGR01409. TAT_signal_seq. 1 hit.
PROSITE	PS00551. MOLYBDOPTERIN_PROK_1. False negative. PS00490. MOLYBDOPTERIN_PROK_2. 1 hit. PS00932. MOLYBDOPTERIN_PROK_3. 1 hit. PS51318. TAT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TORZ_ECOLI

Accession

Primary (citable) accession number: P46923
Secondary accession number(s): P76292, P97187

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1997
Last modified:	November 25, 2008
This is version 74 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)