DMSA_HAEIN
ID DMSA_HAEIN Reviewed; 806 AA.
AC P45004; Q48048;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Dimethyl sulfoxide reductase DmsA;
DE Short=DMSO reductase;
DE Short=DMSOR;
DE Short=Me2SO reductase;
DE EC=1.8.5.3;
DE Flags: Precursor;
GN Name=dmsA; OrderedLocusNames=HI_1047;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Eagan / Serotype B;
RX PubMed=8635740; DOI=10.1016/0378-1119(95)00808-x;
RA Loosmore S.M., Shortreed J.M., Coleman D.C., England D.M., Klein M.H.;
RT "Sequences of the genes encoding the A, B and C subunits of the Haemophilus
RT influenzae dimethylsulfoxide reductase complex.";
RL Gene 169:137-138(1996).
CC -!- FUNCTION: Catalyzes the reduction of dimethyl sulfoxide (DMSO) to
CC dimethyl sulfide (DMS). The terminal DMSO reductase can also use
CC various sulfoxides and N-oxide compounds as terminal electron acceptor
CC in addition to DMSO (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000250};
CC -!- SUBUNIT: Heterotrimeric enzyme composed of a catalytic heterodimer
CC (DmsAB) and a membrane anchor protein (DmsC). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC -!- MISCELLANEOUS: The Tat signal sequence is essential for the expression
CC of dmsA, the stability of the dmsAB dimer and membrane targeting.
CC Despite the presence of a signal sequence, dmsA is not exported to the
CC periplasm (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; L42023; AAC22706.1; -; Genomic_DNA.
DR EMBL; U26665; AAB06233.1; -; Genomic_DNA.
DR PIR; G64109; G64109.
DR RefSeq; NP_439206.1; NC_000907.1.
DR RefSeq; WP_005693382.1; NC_000907.1.
DR AlphaFoldDB; P45004; -.
DR SMR; P45004; -.
DR STRING; 71421.HI_1047; -.
DR EnsemblBacteria; AAC22706; AAC22706; HI_1047.
DR KEGG; hin:HI_1047; -.
DR PATRIC; fig|71421.8.peg.1092; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_6; -.
DR OMA; CPLDCPD; -.
DR PhylomeDB; P45004; -.
DR BioCyc; HINF71421:G1GJ1-1086-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009389; F:dimethyl sulfoxide reductase activity; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0030151; F:molybdenum ion binding; IBA:GO_Central.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
DR InterPro; IPR011888; Anaer_DMSO_reductase.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR TIGRFAMs; TIGR02166; dmsA_ynfE; 1.
DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Cell membrane; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Molybdenum; Oxidoreductase; Reference proteome; Signal.
FT SIGNAL 1..35
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 36..806
FT /note="Dimethyl sulfoxide reductase DmsA"
FT /id="PRO_0000019144"
FT DOMAIN 47..109
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT REGION 786..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 54
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 58
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 62
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 95
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 163..167
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000250"
FT BINDING 196
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 /evidence="ECO:0000250"
FT BINDING 236..237
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000250"
FT BINDING 262..263
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000250"
FT BINDING 283..285
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000250"
FT BINDING 378..379
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000250"
FT BINDING 382
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000250"
FT BINDING 480
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000250"
FT BINDING 504..505
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000250"
FT BINDING 693
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000250"
FT BINDING 699..701
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000250"
FT BINDING 780
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000250"
FT BINDING 796..797
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000250"
FT VARIANT 140
FT /note="D -> Y (in strain: Eagan)"
FT VARIANT 321
FT /note="T -> A (in strain: Eagan)"
FT VARIANT 431
FT /note="V -> M (in strain: Eagan)"
FT VARIANT 440
FT /note="W -> G (in strain: Eagan)"
FT VARIANT 465
FT /note="S -> P (in strain: Eagan)"
FT VARIANT 523
FT /note="T -> P (in strain: Eagan)"
FT VARIANT 724
FT /note="E -> K (in strain: Eagan)"
SQ 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
