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Database: UniProt
Entry: A0A1G8IXX2_9RHOO
LinkDB: A0A1G8IXX2_9RHOO
Original site: A0A1G8IXX2_9RHOO 
ID   A0A1G8IXX2_9RHOO        Unreviewed;       205 AA.
AC   A0A1G8IXX2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Anaerobic dimethyl sulfoxide reductase subunit B (DMSO reductase iron-sulfur subunit) {ECO:0000313|EMBL:SDI23888.1};
GN   ORFNames=SAMN05660652_03085 {ECO:0000313|EMBL:SDI23888.1};
OS   Propionivibrio dicarboxylicus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Propionivibrio.
OX   NCBI_TaxID=83767 {ECO:0000313|EMBL:SDI23888.1, ECO:0000313|Proteomes:UP000198607};
RN   [1] {ECO:0000313|EMBL:SDI23888.1, ECO:0000313|Proteomes:UP000198607}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5885 {ECO:0000313|EMBL:SDI23888.1,
RC   ECO:0000313|Proteomes:UP000198607};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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};
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DR   EMBL; FNCY01000015; SDI23888.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8IXX2; -.
DR   STRING; 83767.SAMN05660652_03085; -.
DR   OrthoDB; 9779457at2; -.
DR   Proteomes; UP000198607; 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   Pfam; PF12797; Fer4_2; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198607}.
FT   DOMAIN          4..34
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          58..88
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          90..119
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          185..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   205 AA;  22248 MW;  2260DA6125B23443 CRC64;
     MTQLGFFVDL SKCTGCKTCQ VACKDKNNLE VGRNFRRVSE YAGGSWKEVH GAWQQDVFAY
     YVSIACNHCA KPACVEVCPK GALAKRADNG LVLIDQQKCI GCRDCEDACP YDAPQYNRAI
     RRMTKCDGCI DRISAGAQPS CVDACPQRAI EFGDVAELRR QHGSLAAVAP LADAATTLPS
     LVLKPSRNSR PVGDTRGTVY PPKAE
//
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