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Database: UniProt
Entry: A0A1Y5SHN6_9PROT
LinkDB: A0A1Y5SHN6_9PROT
Original site: A0A1Y5SHN6_9PROT 
ID   A0A1Y5SHN6_9PROT        Unreviewed;       696 AA.
AC   A0A1Y5SHN6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Dimethyl sulfoxide reductase DmsA {ECO:0000313|EMBL:SLN40930.1};
DE            EC=1.8.5.3 {ECO:0000313|EMBL:SLN40930.1};
GN   Name=dmsA {ECO:0000313|EMBL:SLN40930.1};
GN   ORFNames=OCH7691_01744 {ECO:0000313|EMBL:SLN40930.1};
OS   Oceanibacterium hippocampi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sneathiellales;
OC   Sneathiellaceae; Oceanibacterium.
OX   NCBI_TaxID=745714 {ECO:0000313|EMBL:SLN40930.1, ECO:0000313|Proteomes:UP000193200};
RN   [1] {ECO:0000313|EMBL:SLN40930.1, ECO:0000313|Proteomes:UP000193200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7691 {ECO:0000313|EMBL:SLN40930.1,
RC   ECO:0000313|Proteomes:UP000193200};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (MAR-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}.
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DR   EMBL; FWFR01000001; SLN40930.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y5SHN6; -.
DR   InParanoid; A0A1Y5SHN6; -.
DR   OrthoDB; 9759518at2; -.
DR   Proteomes; UP000193200; Unassembled WGS sequence.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd02766; MopB_3; 1.
DR   CDD; cd02786; MopB_CT_3; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 2.20.25.90; ADC-like domains; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   Gene3D; 3.30.2070.10; Formate dehydrogenase/DMSO reductase; 1.
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; IPR037920; YoaE_C.
DR   PANTHER; PTHR43742:SF6; OXIDOREDUCTASE YYAE-RELATED; 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; PS00490; MOLYBDOPTERIN_PROK_2; 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:0000313|EMBL:SLN40930.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193200}.
FT   DOMAIN          11..69
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   696 AA;  75993 MW;  568AFCC0EEE7CC23 CRC64;
     MAALESTGTT LDFRPSACPH DCPSTCALEV ERLDGRRIGR IRGAADNSYT AGVICAKVAR
     YAERHHHPDR LTRPLRRKGA KGAGEWQTIS WDAALDEVAE NFRALAAKYG SETIWPYFYA
     GTMGLVQRDG INRLRHAMRY SGQYSTICTT LAWTGWIAGT GALMGADPRE MANSDVVVIW
     GTNPVNTQIN VMTHAVKARK NRAAKIVVVD PYRNGTALQA DMHLCLRPGT DGALACAVMH
     VLFRDGYADR DYLKQYTDVP DELEAHLRTR DPAWAAAITG LDEAEITAFA HLLGQNKRSY
     LRLGYGFSRS RNGSINMHAA ASIAAVTGSW RYKGGGAFHN NGAIFHWDRS LIDGLDVRDP
     SIRVLDQSRI GPVLTGDPQD LGDGPPVTGM LIQSTNPMTV APDLAKVHAG FARDDLFVCV
     HEQFMTETAA VADIVLPATT FLEHDDVYQA GGQSHILMGA KVVEPLEGTR SNHEVICGLA
     ERLGARHPGF SMSAREIVDA TLKSSGWGDI ETLEADRWID CAPDFRAAHF LDGFGHPDGK
     FRFAPDWQRL DRQKRDIPRL PDHWTAIDEA TERCPFRMVT APSRNYLNTS FTETPTSIKR
     EGRPSLMLHP DDAARLGLAD GAIARIGNGR GSLRIHVEIF DGVQPGVVVV ESVWPNGAFI
     DGMGINLLTG ADSPAPVGGA AFHDTAIWVE ADDRSA
//
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