ECMDB

Identification

Name:

Anaerobic dimethyl sulfoxide reductase chain A

Synonyms:

DMSO reductase

Gene Name:

dmsA

Enzyme Class:

1.8.5.3

Biological Properties

General Function:

Involved in dimethyl sulfoxide reductase activity

Specific Function:

Terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds. Allows E.coli to grow anaerobically on Me(2)SO as respiratory oxidant

Cellular Location:

Cell membrane; Peripheral membrane protein; Cytoplasmic side

SMPDB Pathways:

Sulfur metabolism PW000922
dimethyl sulfoxide electron transfer PW001892

KEGG Pathways:

Sulfur metabolism ec00920

KEGG Reactions:

1.0

↔

1.0

1.0Menaquinone + 1.0Water + 1.0Dimethyl sulfide ↔ 1.0Menaquinol 6
ReactionCard

SMPDB Reactions:

1.0

2.0

2.0Electron

→

1.0menaquinone-8

1.0

2.0

1.0Menaquinol 8 + 1.0Dimethyl sulfoxide + 2.0Hydrogen ion + 2.0Electron → 1.0menaquinone-8 + 1.0Dimethyl sulfide + 1.0Water + 2.0Hydrogen ion
ReactionCard

Complex Reactions:

1.0

→

1.0

1.0Menaquinone 8

1.0

1.0Hydrogen ion + 1.0Menaquinol 8 + 1.0Trimethylamine N-Oxide → 1.0Water + 1.0Menaquinone 8 + 1.0Trimethylamine
ReactionCard

1.0

→

1.0

1.02-Demethylmenaquinol 8 + 1.0Hydrogen ion + 1.0Trimethylamine N-Oxide → 1.02-Demethylmenaquinone 8 + 1.0Water + 1.0Trimethylamine
ReactionCard

1.0

→

1.0

1.0Menaquinone 8

1.0Dimethyl sulfoxide + 1.0Menaquinol 8 → 1.0Dimethyl sulfide + 1.0Water + 1.0Menaquinone 8
ReactionCard

1.0

→

1.0

1.02-Demethylmenaquinol 8 + 1.0Dimethyl sulfoxide → 1.02-Demethylmenaquinone 8 + 1.0Dimethyl sulfide + 1.0Water
ReactionCard

1.0

→

1.0

1.0Dimethyl sulfide + 1.0Menaquinone + 1.0Water → 1.0Dimethyl sulfoxide + 1.0Menaquinol 6
ReactionCard

Metabolites:

ECMDB ID	Name	View
ECMDB21154	2-Demethylmenaquinol 8	MetaboCard
ECMDB21155	2-Demethylmenaquinone 8	MetaboCard
ECMDB21207	Dimethyl sulfide	MetaboCard
ECMDB21208	Dimethyl sulfoxide	MetaboCard
ECMDB21225	Hydrogen ion	MetaboCard
ECMDB21551	Menaquinol 6	MetaboCard
ECMDB21245	Menaquinol 8	MetaboCard
ECMDB04102	Menaquinone	MetaboCard
ECMDB00906	Trimethylamine	MetaboCard
ECMDB04161	Trimethylamine N-Oxide	MetaboCard
ECMDB00494	Water	MetaboCard

GO Classification:

Function
4 iron, 4 sulfur cluster binding
binding
catalytic activity
cation binding
dimethyl sulfoxide reductase activity
electron carrier activity
ion binding
iron-sulfur cluster binding
metal cluster binding
metal ion binding
molybdenum ion binding
oxidoreductase activity
oxidoreductase activity, acting on a sulfur group of donors
transition metal ion binding
Process
metabolic process
oxidation reduction

Gene Properties

Blattner:

b0894

Gene Orientation

Clockwise

Centisome Percentage:

20.26

Left Sequence End

940182

Right Sequence End

942626

Gene Sequence:

>2445 bp
ATGAAAACGAAAATCCCTGATGCGGTATTGGCTGCTGAGGTGAGTCGCCGTGGTTTGGTA
AAAACGACAGCGATCGGCGGCCTGGCAATGGCCAGCAGCGCATTAACATTACCTTTTAGT
CGGATTGCGCACGCTGTCGATAGCGCCATTCCAACAAAATCAGACGAAAAGGTTATCTGG
AGCGCCTGTACAGTTAACTGTGGTAGTCGCTGCCCGCTACGTATGCACGTCGTGGACGGT
GAAATCAAATATGTCGAAACGGACAATACCGGCGATGACAATTACGACGGCCTGCACCAG
GTTCGCGCCTGCCTGCGTGGGCGTTCCATGCGTCGCCGTGTCTACAATCCGGACCGCCTG
AAATATCCGATGAAACGAGTCGGGGCGCGCGGTGAAGGCAAATTCGAGCGCATTAGCTGG
GAAGAAGCCTACGACATCATCGCGACCAATATGCAGCGCCTGATCAAAGAGTACGGCAAC
GAGTCTATCTATCTGAACTATGGCACCGGTACGCTGGGCGGCACCATGACCCGCTCCTGG
CCGCCGGGAAATACCCTGGTCGCGCGGCTGATGAACTGCTGCGGCGGCTATCTGAACCAT
TACGGCGACTACTCCTCCGCGCAAATTGCGGAAGGTTTGAACTATACCTACGGCGGCTGG
GCAGATGGCAACAGCCCGTCGGATATCGAAAACAGTAAGCTGGTAGTGCTGTTTGGTAAT
AACCCTGGCGAAACGCGAATGAGTGGCGGTGGGGTGACTTACTATCTTGAACAGGCACGC
CAGAAATCTAATGCCCGCATGATCATCATCGATCCGCGCTATACCGACACCGGTGCCGGG
CGCGAAGATGAGTGGATCCCTATTCGTCCGGGAACAGATGCCGCACTGGTTAACGGTCTG
GCGTACGTCATGATCACTGAAAACCTGGTGGATCAGGCATTCCTCGATAAATATTGCGTT
GGCTACGATGAGAAAACCCTGCCAGCCAGTGCGCCGAAAAATGGCCACTATAAAGCTTAT
ATTCTGGGTGAAGGGCCAGATGGCGTGGCTAAAACGCCGGAATGGGCCTCGCAAATCACT
GGTGTTCCGGCAGACAAAATCATCAAATTGGCTCGTGAAATCGGTAGTACCAAACCGGCG
TTTATCAGCCAGGGATGGGGCCCGCAGCGTCACGCTAACGGTGAAATCGCAACCCGTGCT
ATCTCGATGCTGGCGATTCTGACCGGTAACGTTGGTATTAACGGAGGCAACAGCGGCGCG
CGTGAAGGTTCATACAGCTTACCGTTTGTCCGTATGCCGACCTTGGAAAACCCGATCCAG
ACCAGCATTTCGATGTTTATGTGGACCGATGCCATTGAACGTGGCCCGGAAATGACGGCG
CTGCGTGATGGTGTACGCGGGAAAGATAAGCTGGATGTGCCGATCAAAATGATCTGGAAC
TATGCCGGTAACTGCCTGATTAACCAGCATTCTGAAATCAACCGTACCCATGAAATCCTT
CAGGATGATAAGAAGTGCGAGCTGATTGTGGTTATCGACTGCCACATGACCTCATCGGCG
AAATATGCTGACATCCTGCTGCCTGACTGCACCGCTTCCGAACAGATGGACTTTGCGCTG
GATGCATCCTGCGGGAATATGTCTTACGTGATTTTCAACGATCAGGTGATTAAACCGCGC
TTTGAATGTAAGACCATCTATGAAATGACCAGCGAACTGGCAAAACGTCTTGGCGTTGAG
CAACAGTTTACTGAAGGCCGTACCCAGGAAGAGTGGATGCGGCATCTGTATGCCCAGTCG
CGGGAAGCGATTCCTGAACTGCCAACGTTTGAAGAGTTCCGCAAGCAGGGGATCTTTAAA
AAGCGCGACCCACAAGGGCATCACGTTGCTTATAAAGCCTTCCGTGAAGATCCGCAGGCA
AACCCACTGACTACGCCATCGGGCAAAATTGAGATTTATTCGCAGGCGCTGGCTGACATT
GCCGCTACCTGGGAATTGCCTGAAGGCGATGTGATCGATCCACTGCCGATCTACACGCCG
GGCTTTGAAAGTTATCAGGATCCGCTGAACAAACAGTATCCGCTGCAGCTTACAGGTTTC
CACTATAAATCTCGCGTTCACTCAACTTACGGCAACGTTGATGTGCTGAAAGCGGCTTGC
CGTCAGGAAATGTGGATCAACCCGCTTGATGCCCAAAAACGCGGTATCCACAACGGCGAT
AAAGTCAGGATCTTTAACGATCGTGGTGAGGTTCATATTGAGGCGAAAGTGACGCCACGA
ATGATGCCGGGTGTGGTCGCACTGGGTGAAGGTGCCTGGTATGACCCGGATGCAAAACGT
GTCGATAAGGGTGGTTGTATTAACGTACTGACCACTCAACGTCCGTCTCCTCTCGCTAAG
GGGAATCCGTCACATACAAACCTTGTTCAGGTTGAAAAGGTGTAA

Protein Properties

Pfam Domain Function:

Molybdop_Fe4S4 (PF04879 )
Molybdopterin (PF00384 )
Molydop_binding (PF01568 )

Protein Residues:

814

Protein Molecular Weight:

90398

Protein Theoretical pI:

Signaling Regions:

1-45

Transmembrane Regions:

None

Protein Sequence:

>Anaerobic dimethyl sulfoxide reductase chain A
MKTKIPDAVLAAEVSRRGLVKTTAIGGLAMASSALTLPFSRIAHAVDSAIPTKSDEKVIW
SACTVNCGSRCPLRMHVVDGEIKYVETDNTGDDNYDGLHQVRACLRGRSMRRRVYNPDRL
KYPMKRVGARGEGKFERISWEEAYDIIATNMQRLIKEYGNESIYLNYGTGTLGGTMTRSW
PPGNTLVARLMNCCGGYLNHYGDYSSAQIAEGLNYTYGGWADGNSPSDIENSKLVVLFGN
NPGETRMSGGGVTYYLEQARQKSNARMIIIDPRYTDTGAGREDEWIPIRPGTDAALVNGL
AYVMITENLVDQAFLDKYCVGYDEKTLPASAPKNGHYKAYILGEGPDGVAKTPEWASQIT
GVPADKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGGNSGA
REGSYSLPFVRMPTLENPIQTSISMFMWTDAIERGPEMTALRDGVRGKDKLDVPIKMIWN
YAGNCLINQHSEINRTHEILQDDKKCELIVVIDCHMTSSAKYADILLPDCTASEQMDFAL
DASCGNMSYVIFNDQVIKPRFECKTIYEMTSELAKRLGVEQQFTEGRTQEEWMRHLYAQS
REAIPELPTFEEFRKQGIFKKRDPQGHHVAYKAFREDPQANPLTTPSGKIEIYSQALADI
AATWELPEGDVIDPLPIYTPGFESYQDPLNKQYPLQLTGFHYKSRVHSTYGNVDVLKAAC
RQEMWINPLDAQKRGIHNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGAWYDPDAKR
VDKGGCINVLTTQRPSPLAKGNPSHTNLVQVEKV

References

External Links:

Resource	Link
Uniprot ID:	P18775
Uniprot Name:	DMSA_ECOLI
GenBank Gene ID:	AP009048
Genebank Protein ID:	85674786
Ecogene ID:	EG10232
Ecocyc:	EG10232
ColiBase:	b0894
Kegg Gene:	b0894
EchoBASE ID:	EB0228
CCDB:	DMSA_ECOLI
BacMap:	90111183

General Reference:

Bilous, P. T., Cole, S. T., Anderson, W. F., Weiner, J. H. (1988). "Nucleotide sequence of the dmsABC operon encoding the anaerobic dimethylsulphoxide reductase of Escherichia coli." Mol Microbiol 2:785-795. Pubmed: 3062312
Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232
Sambasivarao, D., Scraba, D. G., Trieber, C., Weiner, J. H. (1990). "Organization of dimethyl sulfoxide reductase in the plasma membrane of Escherichia coli." J Bacteriol 172:5938-5948. Pubmed: 2170332
Sambasivarao, D., Turner, R. J., Simala-Grant, J. L., Shaw, G., Hu, J., Weiner, J. H. (2000). "Multiple roles for the twin arginine leader sequence of dimethyl sulfoxide reductase of Escherichia coli." J Biol Chem 275:22526-22531. Pubmed: 10801884
Trieber, C. A., Rothery, R. A., Weiner, J. H. (1994). "Multiple pathways of electron transfer in dimethyl sulfoxide reductase of Escherichia coli." J Biol Chem 269:7103-7109. Pubmed: 8125918
Tullman-Ercek, D., DeLisa, M. P., Kawarasaki, Y., Iranpour, P., Ribnicky, B., Palmer, T., Georgiou, G. (2007). "Export pathway selectivity of Escherichia coli twin arginine translocation signal peptides." J Biol Chem 282:8309-8316. Pubmed: 17218314

Anaerobic dimethyl sulfoxide reductase chain A (P18775)