[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=CMCP6; Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.; "Complete genome sequence of Vibrio vulnificus CMCP6."; Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.

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

AE016795; AAO11229.1; ALT_INIT; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_761702.1; -.

3D structure databases

HSSP

O87948; 1TMO. [HSSP ENTRY / PDB]

ModBase

Q8D8S3.

Enzyme and pathway databases

BioCyc

VVUL216895:VV1_2895-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).

Genome annotation databases

GeneID

1179732; -.

GenomeReviews

AE016795_GR; VV1_2895.

KEGG

vvu:VV1_2895; -.

Phylogenomic databases

HOGENOM

Q8D8S3; -.

Genome annotation databases

CMR

Q8D8S3; VV1_2895.

Other

ProtoNet

Q8D8S3.

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_0000019161`

Sequence information

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

Molecular weight: 92508 Da [This is the MW of the unprocessed precursor]

CRC64: 76231D866025E90C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAITRRSFLK GVATTSAASV IGPSLLASAS ANAVETTGTW KVSGSHWGAF RAHIYAGKVQ 

        70         80         90        100        110        120 
EIKPIELDQN PTEMLNGIKG IIYSPSRVRY PMVRLDWLKK HKYSADTRGN NRFVRVTWDE 

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

       190        200        210        220        230        240 
GAGQTILPYV LGSTEVYAQG TSWSEILENA DNIILWANDP VKNLQVGWNC ETHESYAYLA 

       250        260        270        280        290        300 
QLKEKVAKGE INVISVDPVK NKTQRYLEND HLYVNPMTDV PFMLAIAHVL YTENLYDKKF 

       310        320        330        340        350        360 
IETYCLGFEE FINYVQGKTK DKVEKTPEWA APICGVKADK IREFARMLVK GRTQILMGWC 

       370        380        390        400        410        420 
IQRQEHGEQP YWAAAVVAAM IGQIGLPGGG ISYGHHYSSI GVPSTGFAGP GGFPRNLDAG 

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

       490        500        510        520        530        540 
DRNRMKQAFQ KLQTVVTIDF AWTATCRFSD IVLPACTQWE RNDIDVYGSY SSRGLIAMHR 

       550        560        570        580        590        600 
LVDPLFQSKP DFQIMKELTE RFGRSEEYSR GMSEMDWIRS LYNDCKKSNE GKFEMPEFDE 

       610        620        630        640        650        660 
FWEKSVLDFG QGQPWVRHAD FRQDPEINPL GTPSGFIEIT SRKIGRYGYE HCQEHPMWFE 

       670        680        690        700        710        720 
KSERSHGGPG SDKHPFWLQS CHPDKRLHSQ MCESEEFRAT YAVKGREPVY INPLDAKAKG 

       730        740        750        760        770        780 
IKEGDLVRVF NDRGQLLAGA VLTDSYPRGV IRIEEGAWYG PLNEKVGAID TYGDPNTLTQ 

       790        800        810        820 
DIGSSELAQA TSANTCIVDF EKFTGKVPPV TSFGGPIEVA

Q8D8S3 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