DMSB_HAEIN
ID DMSB_HAEIN Reviewed; 205 AA.
AC P45003; Q48049;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Anaerobic dimethyl sulfoxide reductase chain B;
DE AltName: Full=DMSO reductase iron-sulfur subunit;
GN Name=dmsB; OrderedLocusNames=HI_1046;
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: Electron transfer subunit of the terminal reductase during
CC anaerobic growth on various sulfoxide and N-oxide compounds.
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 4 [4Fe-4S] clusters. {ECO:0000250};
CC -!- SUBUNIT: Heterotrimeric enzyme composed of a catalytic heterodimer
CC (DmsAB) and a membrane anchor protein (DmsC). {ECO:0000250}.
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DR EMBL; L42023; AAC22705.1; -; Genomic_DNA.
DR EMBL; U26665; AAB06234.1; -; Genomic_DNA.
DR PIR; F64109; F64109.
DR RefSeq; NP_439205.1; NC_000907.1.
DR RefSeq; WP_005656008.1; NC_000907.1.
DR AlphaFoldDB; P45003; -.
DR SMR; P45003; -.
DR STRING; 71421.HI_1046; -.
DR EnsemblBacteria; AAC22705; AAC22705; HI_1046.
DR KEGG; hin:HI_1046; -.
DR PATRIC; fig|71421.8.peg.1091; -.
DR eggNOG; COG0437; Bacteria.
DR HOGENOM; CLU_043374_2_0_6; -.
DR OMA; VKPNKHA; -.
DR PhylomeDB; P45003; -.
DR BioCyc; HINF71421:G1GJ1-1085-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR014297; DMSO_DmsB.
DR Pfam; PF13247; Fer4_11; 1.
DR Pfam; PF12800; Fer4_4; 1.
DR TIGRFAMs; TIGR02951; DMSO_dmsB; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
PE 3: Inferred from homology;
KW 4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..205
FT /note="Anaerobic dimethyl sulfoxide reductase chain B"
FT /id="PRO_0000159246"
FT DOMAIN 4..32
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 57..89
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 90..119
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 13
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 16
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 19
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 23
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT VARIANT 60
FT /note="A -> G (in strain: Eagan)"
SQ SEQUENCE 205 AA; 22927 MW; 006A89D0802BF685 CRC64;
MEQYGFYFDS ERCTGCKTCE LACKDYKDLG TEVNFRRIYE YTGGQWNQQA DGCWHQNIFA
YYMSISCNHC ADPACTKVCP TGAMHKNADG FVIVNEEICI GCRYCHMACP YDAPQYDAQK
GHMTKCDGCY SRVKSGQKPI CVDACPLRAL DFAPIDELRT KYGTQASIAP LPPTDITQPN
LVVKPNKYAR LSGDTSGFLG NPREV
