NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=RIMD 2210633 / Serotype O3:K6;
DOI=10.1016/S0140-6736(03)12659-1; PubMed=12620739 [NCBI, ExPASy, EBI, Israel, Japan]
Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae.";
Lancet 361:743-749(2003).

Comments

FUNCTION: Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an anaerobic reaction coupled to energy-yielding reactions (By similarity).
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 (By similarity).
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
SIMILARITY: Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.

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

BA000031; BAC59425.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_797541.1; -.

3D structure databases

HSSP

O87948; 1TMO. [HSSP ENTRY / PDB]

ModBase

Q87QI7.

Enzyme and pathway databases

BioCyc

VPAR223926:VP1162-MON; -.

Ontologies

GO:0042597;	Cellular component: periplasmic space (inferred from electronic annotation from InterPro).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0030151;	Molecular function: molybdenum ion binding (inferred from electronic annotation from InterPro).
GO:0050626;	Molecular function: trimethylamine-N-oxide reductase (cytochrome c) activity (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR009010; Asp_de-COase-like_fold.
IPR006656; Mopterin_OxRdtase.
IPR006655; Mopterin_OxRdtase_prok_CS.
IPR006657; MPT_dinuc_bd.
IPR006311; Tat.
IPR011887; TorA.
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

TIGR01409; TAT_signal_seq; 1.
TIGR02164; torA; 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).

ProtoNet

Q87QI7.

Genome annotation databases

1188667; -.

BA000031_GR; VP1162.

vpa:VP1162; -.

fig|223926.1.peg.1162; -.

Phylogenomic databases

HOGENOM

Q87QI7; -.

Genome annotation databases

CMR

Q87QI7; VP1162.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Molybdenum; Oxidoreductase; Periplasm; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 33`	`33`	`Tat-type signal (Potential).`
`CHAIN`	`34 820`	`787`	`Trimethylamine-N-oxide reductase.`	`PRO_0000019160`

Sequence information

Length: 820 AA [This is the length of the unprocessed precursor]

Molecular weight: 92542 Da [This is the MW of the unprocessed precursor]

CRC64: 9D2E92390C187151 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAITRRSFLK GVATTSAASV IGPSLLASAS ANAAESTGTW KVTGSHWGAF RAHIYAGKVQ 

        70         80         90        100        110        120 
EIKPLELDKN PTEMLNGIKG IIYSPSRVRY PMVRLDWLKK HKYSADTRGN NRFIRVTWDE 

       130        140        150        160        170        180 
ALDLFYRELE RVQKEYGPWA LHAGQTGWNQ TGSFNNCTAH MQRAVGMHGN FITKVGDYST 

       190        200        210        220        230        240 
GAGQTIMPYV LGSTEVYAQG TSWSEILENS DNIILWANDP VKNLQVGWNC ETHESFKYLA 

       250        260        270        280        290        300 
ELKEKVAKGE INVLSVDPVK NKTQRYLEND HLYINPMTDV AFMLAVAHVL YNENLYDKKF 

       310        320        330        340        350        360 
IDTYCLGFEE FIQYVQGKTK DKVEKTPEWA AAICGVKADK IREFARMLVS GRTQILMGWC 

       370        380        390        400        410        420 
IQRQEHGEQP YWAAAVVAAM VGQIGLPGGG ISYGHHYSSI GVPSTGFAGP GGFPRNLDQG 

       430        440        450        460        470        480 
MKPKWDNNDF NGYSRTIPVA RWIDCLLEPG KEINYNGGKV KLPDFKMMVI SGCNPWHHHQ 

       490        500        510        520        530        540 
DRNRMKKAFR KLQTVVTIEF AWTATCRFSD IVLPACTQWE RNDIDVYGSY SNKGLIAMHR 

       550        560        570        580        590        600 
LVDPLFQSKP DFQIMSELTQ RFGRREEYTR GMSEMEWIES LYNDCKKANE GKFEMPEFNE 

       610        620        630        640        650        660 
FWEKSVLDFG EGKPWVRHAD FRKDPELNPL GTPSGFIEIT SRKIGRYGYE HCQEHPMWFE 

       670        680        690        700        710        720 
KSERSHGGPG SDKYPFWLQS CHPDKRLHSQ MCESEEFRAT YAVQGREPVY INPIDAKAKG 

       730        740        750        760        770        780 
IKDGDLVRVF NGRGQLLAGA VLTDSYPRGV IRIEEGAWYG PLNEKEGAIC TYGDPNTLTQ 

       790        800        810        820 
DIGSSELAQA TSANTCIVDF EKFTGKVPPV TSFGGPIEVA

Q87QI7 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools