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Database: UniProt
Entry: I9ARJ8_9FIRM
LinkDB: I9ARJ8_9FIRM
Original site: I9ARJ8_9FIRM 
ID   I9ARJ8_9FIRM            Unreviewed;       193 AA.
AC   I9ARJ8;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Dimethylsulfoxide reductase, chain B {ECO:0000313|EMBL:EIW15572.1};
GN   ORFNames=FB4_1261 {ECO:0000313|EMBL:EIW15572.1};
OS   Pelosinus fermentans B4.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Pelosinus.
OX   NCBI_TaxID=1149862 {ECO:0000313|EMBL:EIW15572.1, ECO:0000313|Proteomes:UP000004324};
RN   [1] {ECO:0000313|EMBL:EIW15572.1, ECO:0000313|Proteomes:UP000004324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:EIW15572.1,
RC   ECO:0000313|Proteomes:UP000004324};
RX   PubMed=22933770; DOI=10.1128/JB.01174-12;
RA   Brown S.D., Podar M., Klingeman D.M., Johnson C.M., Yang Z.K.,
RA   Utturkar S.M., Land M.L., Mosher J.J., Hurt R.A.Jr., Phelps T.J.,
RA   Palumbo A.V., Arkin A.P., Hazen T.C., Elias D.A.;
RT   "Draft Genome Sequences for Two Metal-Reducing Pelosinus fermentans Strains
RT   Isolated from a Cr(VI)-Contaminated Site and for Type Strain R7.";
RL   J. Bacteriol. 194:5147-5148(2012).
CC   -!- FUNCTION: Electron transfer subunit of the terminal reductase during
CC       anaerobic growth on various sulfoxide and N-oxide compounds.
CC       {ECO:0000256|ARBA:ARBA00003584}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EIW15572.1}.
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DR   EMBL; AKVJ01000076; EIW15572.1; -; Genomic_DNA.
DR   RefSeq; WP_007938165.1; NZ_AKVJ01000076.1.
DR   AlphaFoldDB; I9ARJ8; -.
DR   PATRIC; fig|1149862.3.peg.4287; -.
DR   OrthoDB; 9810688at2; -.
DR   Proteomes; UP000004324; Unassembled WGS sequence.
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   CDD; cd16371; DMSOR_beta_like; 1.
DR   Gene3D; 3.30.70.20; -; 2.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR014297; DMSO_DmsB.
DR   NCBIfam; TIGR02951; DMSO_dmsB; 1.
DR   PANTHER; PTHR43177:SF5; ANAEROBIC DIMETHYL SULFOXIDE REDUCTASE CHAIN B-RELATED; 1.
DR   PANTHER; PTHR43177; PROTEIN NRFC; 1.
DR   Pfam; PF13247; Fer4_11; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 3.
PE   4: Predicted;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          5..35
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          58..89
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          91..120
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   193 AA;  21339 MW;  10ACA080FB0D6428 CRC64;
     MSKQIAFYVE QKHCTGCSAC QIACKDKHNL PLGQNFRQIH AYEGGDFTIS GNVVYQNTYA
     YWIPVSCNHC VDASCIAVCP SKAIFKRQED GLVLINEKSC IGCRRCFAVC PYQAPQFDAA
     NGKMKKCDFC QDLLQQGTAP ACVSACPMRV LGYGELSELQ KKYGDTSWVK GLPNTAKIKP
     AWVLVPHRDA VDV
//
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