ID A0A2N5G9Q2_9BACI Unreviewed; 795 AA.
AC A0A2N5G9Q2;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Dimethyl sulfoxide reductase subunit A {ECO:0000313|EMBL:PLR77450.1};
GN ORFNames=CU633_10895 {ECO:0000313|EMBL:PLR77450.1};
OS Bacillus sp. V3-13.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2053728 {ECO:0000313|EMBL:PLR77450.1, ECO:0000313|Proteomes:UP000234805};
RN [1] {ECO:0000313|EMBL:PLR77450.1, ECO:0000313|Proteomes:UP000234805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V3-13 {ECO:0000313|EMBL:PLR77450.1,
RC ECO:0000313|Proteomes:UP000234805};
RA Seuylemezian A., Cooper K., Vaishampayan P.;
RT "Comparitive Functional Genomics of Dry Heat Resistant strains isolated
RT from the Viking Spacecraft.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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:PLR77450.1}.
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DR EMBL; PGUZ01000027; PLR77450.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5G9Q2; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000234805; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0009389; F:dimethyl sulfoxide reductase activity; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR CDD; cd02794; MopB_CT_DmsA-EC; 1.
DR CDD; cd02770; MopB_DmsA-EC; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.12440; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 2.
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; IPR006311; TAT_signal.
DR NCBIfam; TIGR02166; dmsA_ynfE; 1.
DR PANTHER; PTHR43742:SF3; DIMETHYL SULFOXIDE REDUCTASE DMSA; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
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; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000234805};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 53..115
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 795 AA; 88644 MW; 28FE6D8E66F3B513 CRC64;
MSNNLFEKIA NQTMPRRTFL KWTGAITAPA VLGGAVATKH LTEKAKAAES MEDELVIPTC
GTTNCGGRCL VKAHVKNGTI VRITTDDAEE DSLTCPQIRA CIRGRSYRQF VYHPDRLKYP
MKRVGKRGEG KFERISWDEA IETIYKETER ITKKYGPASR YSNYASGNWG GLVSGRVMFN
KLMGLTGGYL GYHNTYSTAQ TNSATPFTYG TASSGSSLDS LVNSKLIILW GHNPAETIWG
TTNFYLKKAK EAGAKIYVVD PRYSDTAVAL ADEWFPIRPT TDNALMDAMT YVIITENLHD
KEFLDKYCIG HDETHMPEGV PEGESLQSYI LGEKDGIAKT PEWAEKICGL SANKIRQLAR
EYATAKPAAL IQGWGPQRNM NGEQIVRGGT VLASLTGNVG VNGGWASGAG YFGRTKIASV
PNVPNPLKLS IPCFLWTDAI IRGTEMSAKD GVLGLKEGET LPSNIKLIFN CAGNALINQH
GDINRTKKIL EDESLVEFIV VSDIFMTPSA KYADILLPSN TFFERYDIGT PWGFGDYAIL
SQKVTDSLYE SKSDYEWMTL LAKKMGLEQE FSQGKTEEDW AKWVIEETRK QDPSFPTWEQ
MKKQGIHKWK FDKPTIGFEE QIKNPDTKPF PTPSGKIEIF SKRLWEMDDP EKIPAIPKHI
AVAEGPEGSL TKKYPLQLIG WHYKRRCHST HDNNVWMEEA SRQEIWMNPI DADKRNIKKG
DVVTVFNDRG IVKIPVAVTN RIIPGVVAIP QGAWYKPDKD GVDTRGCINV LTTLEPSPLA
KGNPQHTNLV EVEKA
//
