DSTOR_CERSP
ID DSTOR_CERSP Reviewed; 822 AA.
AC Q57366; Q53077;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Dimethyl sulfoxide/trimethylamine N-oxide reductase;
DE Short=DMSO reductase;
DE Short=DMSOR;
DE Short=Me2SO reductase;
DE Short=TMAOR;
DE EC=1.7.2.3;
DE EC=1.8.5.3;
DE Flags: Precursor;
GN Name=dmsA; Synonyms=dsrA;
OS Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=1063;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=f. sp. denitrificans IL106;
RX PubMed=8645727; DOI=10.1016/0167-4838(96)00015-5;
RA Hilton J.C., Rajagopalan K.V.;
RT "Molecular cloning of dimethyl sulfoxide reductase from Rhodobacter
RT sphaeroides.";
RL Biochim. Biophys. Acta 1294:111-114(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS, AND
RP PARTIAL PROTEIN SEQUENCE.
RC STRAIN=f. sp. denitrificans IL106;
RX PubMed=8534974; DOI=10.1271/bbb.59.1850;
RA Yamamoto I., Wada N., Ujiiye T., Tachibana M., Matsuzaki M., Kajiwara H.,
RA Watanabe Y., Hirano H., Okubo A., Satoh T., Yamazaki S.;
RT "Cloning and nucleotide sequence of the gene encoding dimethyl sulfoxide
RT reductase from Rhodobacter sphaeroides f. sp. denitrificans.";
RL Biosci. Biotechnol. Biochem. 59:1850-1855(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 53-815, AND PROTEIN SEQUENCE OF
RP 43-815.
RC STRAIN=f. sp. denitrificans IL106;
RX PubMed=7625833; DOI=10.1016/0003-9861(95)90009-8;
RA Barber M.J., van Valkenburgh H., Trimboli A.J., Pollock V.V., Neame P.J.,
RA Bastian N.R.;
RT "The amino acid sequence of Rhodobacter sphaeroides dimethyl sulfoxide
RT reductase.";
RL Arch. Biochem. Biophys. 320:266-275(1995).
RN [4]
RP COFACTOR.
RX PubMed=2326278; DOI=10.1073/pnas.87.8.3190;
RA Johnson J.L., Bastian N.R., Rajagopalan K.V.;
RT "Molybdopterin guanine dinucleotide: a modified form of molybdopterin
RT identified in the molybdenum cofactor of dimethyl sulfoxide reductase from
RT Rhodobacter sphaeroides forma specialis denitrificans.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:3190-3194(1990).
RN [5]
RP SUBCELLULAR LOCATION, AND COFACTOR.
RX PubMed=1710616; DOI=10.1128/jb.173.11.3277-3281.1991;
RA Yoshida Y., Takai M., Satoh T., Takami S.;
RT "Molybdenum requirement for translocation of dimethyl sulfoxide reductase
RT to the periplasmic space in a photodenitrifier, Rhodobacter sphaeroides f.
RT sp. denitrificans.";
RL J. Bacteriol. 173:3277-3281(1991).
RN [6]
RP FUNCTION AS A DIMETHYL SULFOXIDE AND TRIMETHYLAMINE N-OXIDE REDUCTASE, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=9401017; DOI=10.1128/jb.179.24.7617-7624.1997;
RA Mouncey N.J., Choudhary M., Kaplan S.;
RT "Characterization of genes encoding dimethyl sulfoxide reductase of
RT Rhodobacter sphaeroides 2.4.1T: an essential metabolic gene function
RT encoded on chromosome II.";
RL J. Bacteriol. 179:7617-7624(1997).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH COFACTOR.
RX PubMed=8658134; DOI=10.1126/science.272.5268.1615;
RA Schindelin H., Kisker C., Hilton J., Rajagopalan K.V., Rees D.C.;
RT "Crystal structure of DMSO reductase: redox-linked changes in molybdopterin
RT coordination.";
RL Science 272:1615-1621(1996).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH MO-BIS-MGD, COFACTOR,
RP AND SUBUNIT.
RA Li H.-K., Temple C., Rajagopalan K.V., Schindelin H.;
RT "The 1.3 A crystal structure of Rhodobacter sphaeroides dimethyl sulfoxide
RT reductase reveals two distinct molybdenum coordination environments.";
RL J. Am. Chem. Soc. 122:7673-7680(2000).
CC -!- FUNCTION: Catalyzes the reduction of dimethyl sulfoxide (DMSO) and
CC trimethylamine N-oxide (TMAO) to dimethyl sulfide (DMS) and
CC trimethylamine, respectively. The terminal DMSO reductase can also use
CC various sulfoxides and N-oxide compounds as terminal electron acceptor
CC in addition to DMSO and TMAO. {ECO:0000269|PubMed:9401017}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a menaquinone + dimethyl sulfide + H2O = a menaquinol +
CC dimethyl sulfoxide; Xref=Rhea:RHEA:28494, Rhea:RHEA-COMP:9537,
CC Rhea:RHEA-COMP:9539, ChEBI:CHEBI:15377, ChEBI:CHEBI:16374,
CC ChEBI:CHEBI:17437, ChEBI:CHEBI:18151, ChEBI:CHEBI:28262; EC=1.8.5.3;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(III)-[cytochrome c] + H2O + trimethylamine = 2 Fe(II)-
CC [cytochrome c] + 3 H(+) + trimethylamine N-oxide;
CC Xref=Rhea:RHEA:24236, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15724,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:58389; EC=1.7.2.3;
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539;
CC Evidence={ECO:0000269|PubMed:1710616, ECO:0000269|PubMed:2326278,
CC ECO:0000269|Ref.8};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000269|PubMed:1710616,
CC ECO:0000269|PubMed:2326278, ECO:0000269|Ref.8};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8658134, ECO:0000269|Ref.8}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:1710616}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has been experimentally proven.
CC -!- DISRUPTION PHENOTYPE: Disruption of dmsA results in the inability to
CC use DMSO or TMAO as the terminal electron acceptor in anaerobic
CC respiration and in greatly diminished in vitro DMSOR activity.
CC {ECO:0000269|PubMed:9401017}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; L46851; AAB07230.1; -; Genomic_DNA.
DR EMBL; D38634; BAA07615.1; -; Genomic_DNA.
DR EMBL; U25037; AAC13660.1; -; Genomic_DNA.
DR PIR; S70012; S70012.
DR PDB; 1EU1; X-ray; 1.30 A; A=43-822.
DR PDBsum; 1EU1; -.
DR AlphaFoldDB; Q57366; -.
DR SMR; Q57366; -.
DR DrugBank; DB02153; 3-sulfino-L-alanine.
DR DrugBank; DB02379; Beta-D-Glucose.
DR EvolutionaryTrace; Q57366; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0050626; F:trimethylamine-N-oxide reductase (cytochrome c) activity; IEA:UniProtKB-EC.
DR CDD; cd02793; MopB_CT_DMSOR-BSOR-TMAOR; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006658; BisC.
DR InterPro; IPR041954; CT_DMSOR/BSOR/TMAOR.
DR InterPro; IPR041460; Molybdopterin_N.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF18364; Molybdopterin_N; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR TIGRFAMs; TIGR00509; bisC_fam; 1.
DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Metal-binding; Molybdenum;
KW Oxidoreductase; Periplasm; Signal.
FT SIGNAL 1..42
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:7625833, ECO:0000269|PubMed:8534974"
FT CHAIN 43..822
FT /note="Dimethyl sulfoxide/trimethylamine N-oxide reductase"
FT /id="PRO_0000019146"
FT BINDING 158..160
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 158
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 189
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT BINDING 232..233
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 262..263
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 283..285
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 364..365
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 368
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 476
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 480
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 500..501
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 523
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 553
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 683..686
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 689
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 691..693
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 779
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 796..797
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT CONFLICT 185
FT /note="S -> V (in Ref. 3; AAC13660)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="A -> G (in Ref. 3; AAC13660)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="H -> Y (in Ref. 3; AAC13660)"
FT /evidence="ECO:0000305"
FT CONFLICT 371..373
FT /note="HGE -> MAQ (in Ref. 3; AAC13660)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="G -> A (in Ref. 3; AAC13660)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="W -> C (in Ref. 3; AAC13660)"
FT /evidence="ECO:0000305"
FT CONFLICT 695
FT /note="N -> T (in Ref. 3; AAC13660)"
FT /evidence="ECO:0000305"
FT CONFLICT 706
FT /note="A -> V (in Ref. 3; AAC13660)"
FT /evidence="ECO:0000305"
FT CONFLICT 742
FT /note="A -> T (in Ref. 3; AAC13660)"
FT /evidence="ECO:0000305"
FT CONFLICT 749
FT /note="M -> I (in Ref. 3; AAC13660)"
FT /evidence="ECO:0000305"
FT CONFLICT 793
FT /note="G -> D (in Ref. 3; AAC13660)"
FT /evidence="ECO:0000305"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 84..89
FT /evidence="ECO:0007829|PDB:1EU1"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 104..109
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 128..146
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 167..178
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 193..200
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 213..219
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 244..255
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 258..265
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 268..273
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 285..298
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 304..310
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 314..321
FT /evidence="ECO:0007829|PDB:1EU1"
FT TURN 322..326
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 332..339
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 343..354
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:1EU1"
FT TURN 370..373
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 374..386
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 395..398
FT /evidence="ECO:0007829|PDB:1EU1"
FT TURN 403..406
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 437..440
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 441..443
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 444..449
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 454..457
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 460..463
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 469..474
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 477..480
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 484..490
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 491..493
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 495..503
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 506..509
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 512..517
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 520..522
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 525..529
FT /evidence="ECO:0007829|PDB:1EU1"
FT TURN 531..533
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 536..540
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 553..563
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 567..571
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 576..593
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 601..607
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 609..611
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 616..619
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 624..628
FT /evidence="ECO:0007829|PDB:1EU1"
FT TURN 630..632
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 640..645
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 647..652
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 677..682
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 687..690
FT /evidence="ECO:0007829|PDB:1EU1"
FT TURN 694..696
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 698..702
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 710..713
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 715..719
FT /evidence="ECO:0007829|PDB:1EU1"
FT TURN 720..722
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 728..732
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 737..744
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 752..754
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 773..775
FT /evidence="ECO:0007829|PDB:1EU1"
FT HELIX 778..780
FT /evidence="ECO:0007829|PDB:1EU1"
FT TURN 789..791
FT /evidence="ECO:0007829|PDB:1EU1"
FT STRAND 800..805
FT /evidence="ECO:0007829|PDB:1EU1"
SQ SEQUENCE 822 AA; 89208 MW; 4AB3497E5D26B1C9 CRC64;
MTKLSGQELH AELSRRAFLS YTAAVGALGL CGTSLLAQGA RAEGLANGEV MSGCHWGVFK
ARVENGRAVA FEPWDKDPAP SHQLPGVLDS IYSPTRIKYP MVRREFLEKG VNADRSTRGN
GDFVRVTWDE ALDLVARELK RVQESYGPTG TFGGSYGWKS PGRLHNCQVL MRRALNLAGG
FVNSSGDYST AAAQIIMPHV MGTLEVYEQQ TAWPVVVENT DLMVFWAADP MKTNEIGWVI
PDHGAYAGMK ALKEKGTRVI CINPVRTETA DYFGADVVSP RPQTDVALML GMAHTLYSED
LHDKDFLENC TTGFDLFAAY LTGESDGTPK TAEWAAEICG LPAEQIRELA RSFVAGRTML
AAGWSIQRMH HGEQAHWMLV TLASMIGQIG LPGGGFGLSY HYSNGGSPTS DGPALGGISD
GGKAVEGAAW LSESGATSIP CARVVDMLLN PGGEFQFNGA TATYPDVKLA YWAGGNPFAH
HQDRNRMLKA WEKLETFIVQ DFQWTATARH ADIVLPATTS YERNDIESVG DYSNRAILAM
KKVVDPLYEA RSDYDIFAAL AERLGKGAEF TEGRDEMGWI SSFYEAAVKQ AEFKNVAMPS
FEDFWSEGIV EFPITEGANF VRYADFREDP LFNPLGTPSG LIEIYSKNIE KMGYDDCPAH
PTWMEPAERL GGAGAKYPLH VVASHPKSRL HSQLNGTSLR DLYAVAGHEP CLINPADAAA
RGIADGDVLR VFNDRGQILV GAKVSDAVMP GAIQIYEGGW YDPLDPSEEG TLDKYGDVNV
LSLDVGTSKL AQGNCGQTIL ADVEKYAGAP VTVTVFDTPK GA
