DDHB_RHOSU
ID DDHB_RHOSU Reviewed; 325 AA.
AC Q8GPG3;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Dimethylsulfide dehydrogenase subunit beta;
DE Short=DMS DH subunit beta;
DE AltName: Full=DMS DH iron-sulfur subunit;
DE AltName: Full=Dimethyl sulfide:cytochrome c2 reductase subunit beta;
DE AltName: Full=Dimethylsulfide iron-sulfur subunit;
GN Name=ddhB;
OS Rhodovulum sulfidophilum (Rhodobacter sulfidophilus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodovulum.
OX NCBI_TaxID=35806;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SH1;
RX PubMed=12067345; DOI=10.1046/j.1365-2958.2002.02978.x;
RA McDevitt C.A., Hugenholtz P., Hanson G.R., McEwan A.G.;
RT "Molecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum
RT sulfidophilum: its place in the dimethyl sulphoxide reductase family of
RT microbial molybdopterin-containing enzymes.";
RL Mol. Microbiol. 44:1575-1587(2002).
RN [2]
RP FUNCTION, SUBUNIT, AND COFACTOR.
RX PubMed=8706745; DOI=10.1111/j.1432-1033.1996.0391u.x;
RA Hanlon S.P., Toh T.H., Solomon P.S., Holt R.A., McEwan A.G.;
RT "Dimethylsulfide:acceptor oxidoreductase from Rhodobacter sulfidophilus.
RT The purified enzyme contains b-type haem and a pterin molybdenum
RT cofactor.";
RL Eur. J. Biochem. 239:391-396(1996).
CC -!- FUNCTION: Electron transfer subunit of the dehydrogenase during
CC anaerobic growth on dimethyl sulfide. {ECO:0000250,
CC ECO:0000269|PubMed:8706745}.
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000250};
CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 3 [4Fe-4S] clusters. {ECO:0000250};
CC -!- SUBUNIT: Heterotrimer of alpha, beta and gamma subunits.
CC {ECO:0000269|PubMed:8706745}.
CC -!- SUBCELLULAR LOCATION: Periplasm. Note=Probably translocated together
CC with DdhA, which possesses a Tat-type signal.
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DR EMBL; AF453479; AAN46633.1; -; Genomic_DNA.
DR RefSeq; WP_060833690.1; NZ_MSYR01000001.1.
DR AlphaFoldDB; Q8GPG3; -.
DR SMR; Q8GPG3; -.
DR STRING; 1188256.BASI01000002_gene2972; -.
DR KEGG; ag:AAN46633; -.
DR eggNOG; COG1140; Bacteria.
DR OrthoDB; 1762646at2; -.
DR BioCyc; MetaCyc:MON-14243; -.
DR BRENDA; 1.8.2.4; 5384.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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 GO; GO:0009061; P:anaerobic respiration; IEA:InterPro.
DR CDD; cd10555; EBDH_beta; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017839; DMSO_Rdtase_II_Fe-S_su.
DR Pfam; PF13247; Fer4_11; 1.
DR TIGRFAMs; TIGR03478; DMSO_red_II_bet; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
PE 1: Evidence at protein level;
KW 3Fe-4S; 4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Periplasm; Repeat; Transport.
FT CHAIN 1..325
FT /note="Dimethylsulfide dehydrogenase subunit beta"
FT /id="PRO_0000159292"
FT DOMAIN 6..35
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 123..154
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 156..185
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 15
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 18
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 21
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 25
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 325 AA; 37026 MW; F62990FBD394E727 CRC64;
MVKRQISMVL DLNKCIGCQT CTSACKLQWT NRNGREYMYW NNVETHPGPG YPRNYEHSGG
GFDEEGALKI GITPSAEDYG IPWEYNYEEA LMTGTDPWLR PNVKPTWGAN WNEDEGRGEY
PNSYYFYLPR ICNHCANPGC LAACARNAIY KRQEDGIVLV DQERCRGYRY CITACPYKKV
YFNEQISKAE KCIFCYPRIE KGLPTACAKQ CVGRIRFIGY LDDEAGPVHL LVERYKVAIP
LHPEWGTKPS VFYVPPLAPP RIGDDGEPTE ETRVPLAYLK ELFGEAVVPA LETLKTERAK
KQSGAESELM DTLIGYRHPE MFKLS
