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Dimethyl sulfoxide reductase DmsA (DMSO reductase) (DMSOR) (Me2SO reductase) (EC 1.8.5.3)

 DMSA_HAEIN              Reviewed;         806 AA.
P45004; Q48048;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
28-FEB-2018, entry version 132.
RecName: Full=Dimethyl sulfoxide reductase DmsA;
Short=DMSO reductase;
Short=DMSOR;
Short=Me2SO reductase;
EC=1.8.5.3;
Flags: Precursor;
Name=dmsA; OrderedLocusNames=HI_1047;
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
Pasteurellaceae; Haemophilus.
NCBI_TaxID=71421;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
PubMed=7542800; DOI=10.1126/science.7542800;
Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M.,
Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D.,
Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C.,
Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M.,
Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O.,
Venter J.C.;
"Whole-genome random sequencing and assembly of Haemophilus influenzae
Rd.";
Science 269:496-512(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Eagan / Serotype B;
PubMed=8635740; DOI=10.1016/0378-1119(95)00808-X;
Loosmore S.M., Shortreed J.M., Coleman D.C., England D.M., Klein M.H.;
"Sequences of the genes encoding the A, B and C subunits of the
Haemophilus influenzae dimethylsulfoxide reductase complex.";
Gene 169:137-138(1996).
-!- FUNCTION: Catalyzes the reduction of dimethyl sulfoxide (DMSO) to
dimethyl sulfide (DMS). The terminal DMSO reductase can also use
various sulfoxides and N-oxide compounds as terminal electron
acceptor in addition to DMSO (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Dimethylsulfide + menaquinone + H(2)O =
dimethylsulfoxide + menaquinol.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000305};
Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
-!- COFACTOR:
Name=Mo-bis(molybdopterin guanine dinucleotide);
Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250};
Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide)
(Mo-bis-MGD) cofactor per subunit. {ECO:0000250};
-!- SUBUNIT: Heterotrimeric enzyme composed of a catalytic heterodimer
(DmsAB) and a membrane anchor protein (DmsC). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral
membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
-!- PTM: Predicted to be exported by the Tat system. The position of
the signal peptide cleavage has not been experimentally proven.
-!- MISCELLANEOUS: The Tat signal sequence is essential for the
expression of dmsA, the stability of the dmsAB dimer and membrane
targeting. Despite the presence of a signal sequence, dmsA is not
exported to the periplasm (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
oxidoreductase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L42023; AAC22706.1; -; Genomic_DNA.
EMBL; U26665; AAB06233.1; -; Genomic_DNA.
PIR; G64109; G64109.
RefSeq; NP_439206.1; NC_000907.1.
RefSeq; WP_005693382.1; NC_000907.1.
ProteinModelPortal; P45004; -.
SMR; P45004; -.
STRING; 71421.HI1047; -.
EnsemblBacteria; AAC22706; AAC22706; HI_1047.
GeneID; 950024; -.
KEGG; hin:HI1047; -.
PATRIC; fig|71421.8.peg.1092; -.
eggNOG; ENOG4107QY8; Bacteria.
eggNOG; COG0243; LUCA.
KO; K07306; -.
OMA; HYGDYST; -.
PhylomeDB; P45004; -.
BioCyc; HINF71421:G1GJ1-1086-MONOMER; -.
Proteomes; UP000000579; Chromosome.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0009389; F:dimethyl sulfoxide reductase activity; IEA:InterPro.
GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
InterPro; IPR011888; Anaer_DMSO_reductase.
InterPro; IPR009010; Asp_de-COase-like_dom_sf.
InterPro; IPR006657; MoPterin_dinucl-bd_dom.
InterPro; IPR006656; Mopterin_OxRdtase.
InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
InterPro; IPR006311; TAT_signal.
InterPro; IPR019546; TAT_signal_bac_arc.
Pfam; PF04879; Molybdop_Fe4S4; 1.
Pfam; PF00384; Molybdopterin; 1.
Pfam; PF01568; Molydop_binding; 1.
SMART; SM00926; Molybdop_Fe4S4; 1.
SUPFAM; SSF50692; SSF50692; 1.
TIGRFAMs; TIGR02166; dmsA_ynfE; 1.
TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PROSITE; PS51318; TAT; 1.
3: Inferred from homology;
4Fe-4S; Cell membrane; Complete proteome; Iron; Iron-sulfur; Membrane;
Metal-binding; Molybdenum; Oxidoreductase; Reference proteome; Signal.
SIGNAL 1 35 Tat-type signal. {ECO:0000255|PROSITE-
ProRule:PRU00648}.
CHAIN 36 806 Dimethyl sulfoxide reductase DmsA.
/FTId=PRO_0000019144.
DOMAIN 47 109 4Fe-4S Mo/W bis-MGD-type.
{ECO:0000255|PROSITE-ProRule:PRU01004}.
REGION 163 167 MGD 1 binding. {ECO:0000250}.
REGION 236 237 MGD 2 binding. {ECO:0000250}.
REGION 262 263 MGD 2 binding. {ECO:0000250}.
REGION 283 285 MGD 2 binding. {ECO:0000250}.
REGION 378 379 MGD 2 binding. {ECO:0000250}.
REGION 504 505 MGD 1 binding. {ECO:0000250}.
REGION 693 693 MGD 1 binding. {ECO:0000250}.
REGION 699 701 MGD 1 binding. {ECO:0000250}.
REGION 796 797 MGD 1 binding. {ECO:0000250}.
METAL 54 54 Iron-sulfur (4Fe-4S).
{ECO:0000255|PROSITE-ProRule:PRU01004}.
METAL 58 58 Iron-sulfur (4Fe-4S).
{ECO:0000255|PROSITE-ProRule:PRU01004}.
METAL 62 62 Iron-sulfur (4Fe-4S).
{ECO:0000255|PROSITE-ProRule:PRU01004}.
METAL 95 95 Iron-sulfur (4Fe-4S).
{ECO:0000255|PROSITE-ProRule:PRU01004}.
METAL 196 196 Molybdenum. {ECO:0000250}.
BINDING 382 382 Molybdopterin guanine dinucleotide 1.
{ECO:0000250}.
BINDING 480 480 Molybdopterin guanine dinucleotide 1.
{ECO:0000250}.
BINDING 780 780 Molybdopterin guanine dinucleotide 1.
{ECO:0000250}.
VARIANT 140 140 D -> Y (in strain: Eagan).
VARIANT 321 321 T -> A (in strain: Eagan).
VARIANT 431 431 V -> M (in strain: Eagan).
VARIANT 440 440 W -> G (in strain: Eagan).
VARIANT 465 465 S -> P (in strain: Eagan).
VARIANT 523 523 T -> P (in strain: Eagan).
VARIANT 724 724 E -> K (in strain: Eagan).
SEQUENCE 806 AA; 90427 MW; F9F90E5EB250FFBF CRC64;
MSNFNQISRR DFVKASSAGA ALAVSNLTLP FNVMAKETQR LNENNQERIV WSACTVNCGS
RCPLRMHVKD NRITYVETDN TGTETYNLDH QVRACLRGRS MRRRVYNPDR LKYPMKRIGK
RGEGKFKRIS WDEALTEIAD ALKRNIKKYG NESIYLNYGT GTLGGTMAKS WPPASTMIAR
FMNCIGGYLN HYGDYSTAQI AVGLDYTYGG GWALGNGMAD IENTKLIVLF GNNPAETRMS
GGGLTYCIEQ AKARSNAKMI IIDPRYNDTG AGREDEWIPI RPGTDAALVA ALAYVMIQEN
LVDQPFLDKY CVGYDEKTLP TDAPKNGHYK AYILGYGNDG IAKTPEWAAK ITGIPAERII
KLAREIGSTK PAFISQGWGP QRRSNGELIS RAIAMLPILT GNVGIHGGNT GARESAYSIP
FVRMPTLKNP VKASIPMFLW TDAIIRGTEM TALTDGIRGV DKLSSPIKVI WNYASNCLIN
QHAQINRTHD ILQDDTQCEM IITIDNHMTS TAKYSDILLP DCTTSEQMDF ALDAFVSNMA
YVIFADQVIK PSFECRPIYD MLSDLAEKMG VKEKFTEGRT QEEWLRHIYE QSREKLPELP
TFEEFRQQGI FKKVDPNGFK VAYKDFRDNP EAHPLKTPSG KIEIYSSRLA EIAKTWKLAE
DDVIHPLPIH AQSFEHYGDP LMEKYPLQLS GFHYKARTHS TYGNVDVLKA ANPQEVWMNP
IDAEPRNIKN GDMIRIFNDR GEVHINVKIT PRIIPGVVAL SEGAWYAPDK DRIDHSGCIN
VLTTQRPSPL AKGNPQHSNL VQVERL


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