Dimethyl sulfoxide/trimethylamine N-oxide reductase
Details
- Name
- Dimethyl sulfoxide/trimethylamine N-oxide reductase
- Synonyms
- 1.7.2.3
- DMSO reductase
- dsrA
- Gene Name
- dmsA
- Organism
- Rhodobacter sphaeroides
- Amino acid sequence
>lcl|BSEQ0011050|Dimethyl sulfoxide/trimethylamine N-oxide reductase MTKLSGQELHAELSRRAFLSYTAAVGALGLCGTSLLAQGARAEGLANGEVMSGCHWGVFK ARVENGRAVAFEPWDKDPAPSHQLPGVLDSIYSPTRIKYPMVRREFLEKGVNADRSTRGN GDFVRVTWDEALDLVARELKRVQESYGPTGTFGGSYGWKSPGRLHNCQVLMRRALNLAGG FVNSSGDYSTAAAQIIMPHVMGTLEVYEQQTAWPVVVENTDLMVFWAADPMKTNEIGWVI PDHGAYAGMKALKEKGTRVICINPVRTETADYFGADVVSPRPQTDVALMLGMAHTLYSED LHDKDFLENCTTGFDLFAAYLTGESDGTPKTAEWAAEICGLPAEQIRELARSFVAGRTML AAGWSIQRMHHGEQAHWMLVTLASMIGQIGLPGGGFGLSYHYSNGGSPTSDGPALGGISD GGKAVEGAAWLSESGATSIPCARVVDMLLNPGGEFQFNGATATYPDVKLAYWAGGNPFAH HQDRNRMLKAWEKLETFIVQDFQWTATARHADIVLPATTSYERNDIESVGDYSNRAILAM KKVVDPLYEARSDYDIFAALAERLGKGAEFTEGRDEMGWISSFYEAAVKQAEFKNVAMPS FEDFWSEGIVEFPITEGANFVRYADFREDPLFNPLGTPSGLIEIYSKNIEKMGYDDCPAH PTWMEPAERLGGAGAKYPLHVVASHPKSRLHSQLNGTSLRDLYAVAGHEPCLINPADAAA RGIADGDVLRVFNDRGQILVGAKVSDAVMPGAIQIYEGGWYDPLDPSEEGTLDKYGDVNV LSLDVGTSKLAQGNCGQTILADVEKYAGAPVTVTVFDTPKGA
- Number of residues
- 822
- Molecular Weight
- 89206.805
- Theoretical pI
- 4.87
- GO Classification
- Functionselectron carrier activity / molybdenum ion binding / trimethylamine-N-oxide reductase (cytochrome c) activityComponentsperiplasmic space
- General Function
- Trimethylamine-n-oxide reductase (cytochrome c) activity
- Specific Function
- Catalyzes the reduction of dimethyl sulfoxide (DMSO) and trimethylamine N-oxide (TMAO) to dimethyl sulfide (DMS) and trimethylamine, respectively. The terminal DMSO reductase can also use various sulfoxides and N-oxide compounds as terminal electron acceptor in addition to DMSO and TMAO.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Periplasm
- Gene sequence
>lcl|BSEQ0002947|2469 bp ATGACGAAGTTGTCAGGTCAGGAGCTGCATGCCGAACTCTCGCGGCGCGCCTTCCTGAGC TATACGGCGGCGGTGGGGGCTCTCGGTCTCTGCGGCACCTCGCTCCTCGCGCAGGGGGCC CGCGCGGAAGGTCTCGCCAATGGCGAGGTCATGTCGGGCTGCCACTGGGGCGTGTTCAAG GCCCGGGTCGAGAACGGCCGCGCCGTGGCCTTCGAGCCCTGGGACAAGGATCCCGCGCCG TCGCACCAGCTGCCGGGCGTGCTCGATTCGATCTATTCGCCCACGCGGATCAAATATCCG ATGGTGCGCCGCGAGTTCCTCGAGAAGGGCGTGAACGCCGATCGCTCGACCCGCGGCAAC GGCGATTTCGTCCGCGTCACCTGGGATGAGGCGCTCGACCTCGTGGCCCGCGAGCTGAAG CGCGTTCAGGAGAGCTACGGCCCCACCGGCACCTTCGGCGGCTCCTACGGCTGGAAGAGC CCGGGCCGGCTGCACAATTGTCAGGTCCTCATGCGCCGCGCGCTGAATCTGGCGGGCGGG TTCGTGAACTCGTCGGGCGACTATTCGACGGCGGCCGCGCAGATCATCATGCCGCATGTC ATGGGCACGCTCGAGGTCTACGAGCAGCAGACCGCCTGGCCCGTGGTGGTGGAGAACACC GATCTTATGGTCTTCTGGGCCGCCGACCCGATGAAGACCAACGAGATCGGCTGGGTGATC CCCGACCATGGCGCCTATGCCGGCATGAAGGCCCTGAAGGAGAAGGGCACCAGGGTCATC TGCATCAACCCCGTGCGCACCGAGACGGCCGACTATTTCGGCGCCGACGTCGTGTCGCCC CGGCCGCAGACCGACGTGGCGCTGATGCTCGGCATGGCGCACACGCTCTACAGCGAAGAC CTGCACGACAAGGACTTCCTCGAGAACTGCACCACGGGCTTCGACCTCTTCGCGGCCTAC CTGACCGGCGAGAGCGACGGCACGCCCAAGACGGCCGAATGGGCCGCCGAGATCTGCGGC CTGCCGGCCGAGCAGATCAGGGAGCTCGCCCGCAGCTTCGTGGCCGGCCGGACGATGCTC GCCGCGGGCTGGTCGATCCAGCGGATGCACCATGGCGAACAGGCGCACTGGATGCTCGTG ACTCTGGCCTCGATGATCGGCCAGATCGGTCTGCCGGGCGGCGGCTTCGGCCTCAGCTAC CACTATTCGAACGGCGGCTCGCCCACGAGCGACGGCCCGGCGCTGGGCGGGATCTCGGAC GGCGGCAAGGCGGTCGAAGGCGCGGCCTGGCTGTCGGAGAGCGGCGCGACCTCGATCCCC TGCGCCCGCGTGGTAGACATGCTGCTCAATCCGGGCGGCGAGTTCCAGTTCAACGGCGCC ACGGCGACCTATCCCGACGTGAAGCTGGCCTACTGGGCGGGCGGCAACCCCTTCGCGCAC CACCAGGACCGCAACCGGATGCTCAAGGCCTGGGAAAAGCTCGAGACCTTCATCGTGCAG GACTTCCAGTGGACCGCAACCGCGCGCCACGCCGACATCGTCCTGCCGGCGACGACCTCC TACGAGCGCAACGACATCGAGTCGGTGGGCGACTATTCGAACCGCGCCATCCTCGCGATG AAGAAGGTGGTCGATCCGCTCTACGAGGCCCGGTCGGACTACGACATCTTCGCAGCCCTG GCCGAGCGCCTGGGCAAGGGCGCCGAATTCACCGAAGGGCGCGACGAGATGGGGTGGATC AGCTCGTTCTACGAGGCTGCGGTGAAGCAGGCGGAGTTCAAGAACGTGGCGATGCCGTCG TTCGAGGATTTCTGGTCGGAAGGGATCGTCGAATTCCCGATCACCGAGGGCGCGAACTTC GTCCGCTATGCCGACTTCCGCGAGGATCCGCTGTTCAACCCGCTCGGCACGCCCTCGGGC CTGATCGAGATCTACTCGAAGAACATCGAGAAGATGGGCTATGACGATTGCCCGGCCCAT CCGACCTGGATGGAACCGGCCGAGCGTCTCGGCGGGGCAGGGGCGAAATATCCGCTCCAT GTCGTGGCGAGCCATCCGAAGTCGCGGCTGCACTCGCAGCTGAACGGCACCTCGCTGCGC GACCTCTATGCGGTGGCGGGGCACGAACCCTGCCTCATCAACCCCGCCGATGCGGCCGCG CGCGGCATCGCGGACGGCGATGTGCTGCGGGTGTTCAACGACCGCGGGCAGATCCTCGTG GGGGCGAAGGTCAGCGACGCGGTGATGCCGGGCGCGATCCAGATCTACGAGGGCGGCTGG TACGACCCGCTCGATCCCTCGGAGGAGGGCACGCTCGACAAGTACGGCGACGTGAACGTG CTGTCGCTCGATGTCGGCACCTCGAAGCTGGCGCAGGGCAACTGCGGCCAGACCATCCTC GCGGATGTCGAGAAATATGCGGGCGCGCCGGTGACGGTGACCGTGTTCGACACGCCGAAG GGCGCCTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q57366 UniProtKB Entry Name DSTOR_RHOSH GenBank Protein ID 1161236 GenBank Gene ID L46851 - General References
- Hilton JC, Rajagopalan KV: Molecular cloning of dimethyl sulfoxide reductase from Rhodobacter sphaeroides. Biochim Biophys Acta. 1996 May 23;1294(2):111-4. [Article]
- Yamamoto I, Wada N, Ujiiye T, Tachibana M, Matsuzaki M, Kajiwara H, Watanabe Y, Hirano H, Okubo A, Satoh T, et al.: Cloning and nucleotide sequence of the gene encoding dimethyl sulfoxide reductase from Rhodobacter sphaeroides f. sp. denitrificans. Biosci Biotechnol Biochem. 1995 Oct;59(10):1850-5. [Article]
- Barber MJ, Van Valkenburgh H, Trimboli AJ, Pollock VV, Neame PJ, Bastian NR: The amino acid sequence of Rhodobacter sphaeroides dimethyl sulfoxide reductase. Arch Biochem Biophys. 1995 Jul 10;320(2):266-75. [Article]
- Johnson JL, Bastian NR, Rajagopalan KV: Molybdopterin guanine dinucleotide: a modified form of molybdopterin identified in the molybdenum cofactor of dimethyl sulfoxide reductase from Rhodobacter sphaeroides forma specialis denitrificans. Proc Natl Acad Sci U S A. 1990 Apr;87(8):3190-4. [Article]
- Yoshida Y, Takai M, Satoh T, Takami S: Molybdenum requirement for translocation of dimethyl sulfoxide reductase to the periplasmic space in a photodenitrifier, Rhodobacter sphaeroides f. sp. denitrificans. J Bacteriol. 1991 Jun;173(11):3277-81. [Article]
- Mouncey NJ, Choudhary M, Kaplan S: Characterization of genes encoding dimethyl sulfoxide reductase of Rhodobacter sphaeroides 2.4.1T: an essential metabolic gene function encoded on chromosome II. J Bacteriol. 1997 Dec;179(24):7617-24. [Article]
- Schindelin H, Kisker C, Hilton J, Rajagopalan KV, Rees DC: Crystal structure of DMSO reductase: redox-linked changes in molybdopterin coordination. Science. 1996 Jun 14;272(5268):1615-21. [Article]