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Database: UniProt
Entry: A0A1Y2N738_PSEAH
LinkDB: A0A1Y2N738_PSEAH
Original site: A0A1Y2N738_PSEAH 
ID   A0A1Y2N738_PSEAH        Unreviewed;       715 AA.
AC   A0A1Y2N738;
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:OSY42907.1};
DE            EC=1.8.5.3 {ECO:0000313|EMBL:OSY42907.1};
GN   Name=dmsA_1 {ECO:0000313|EMBL:OSY42907.1};
GN   ORFNames=BG845_01149 {ECO:0000313|EMBL:OSY42907.1};
OS   Pseudonocardia autotrophica (Amycolata autotrophica) (Nocardia
OS   autotrophica).
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=2074 {ECO:0000313|EMBL:OSY42907.1, ECO:0000313|Proteomes:UP000194360};
RN   [1] {ECO:0000313|EMBL:OSY42907.1, ECO:0000313|Proteomes:UP000194360}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 535 {ECO:0000313|EMBL:OSY42907.1,
RC   ECO:0000313|Proteomes:UP000194360};
RA   Grumaz C., Vainshtein Y., Kirstahler P., Sohn K.;
RT   "Pseudonocardia autotrophica DSM535, a candidate organism with high
RT   potential of specific P450 cytochromes.";
RL   Submitted (SEP-2016) 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:OSY42907.1}.
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DR   EMBL; MIGB01000004; OSY42907.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2N738; -.
DR   STRING; 2074.BG845_01149; -.
DR   OrthoDB; 7376058at2; -.
DR   Proteomes; UP000194360; 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   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   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:OSY42907.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194360}.
FT   DOMAIN          10..68
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   715 AA;  77094 MW;  B07158484D3AE00C CRC64;
     MTTTDDRPTS TTVRAACPQD CPDTCAMLVT VDGDGKATSV VGDPDHPYTN GGLCVKVNNY
     LDRVYDPGRV LFPMRRTGPK GSGRFERITW DDAVTEIATR FKAIADEHGP EAIMPVSYLG
     TQGILNGLNV GDPFFAKLGA TVAERTYCDS GSCTAYAMTI GDTAGVDPES LVHSTFILVW
     ACNIMSTNLH LWPYIAKAKK NGAKVVVVDP IRTRTAAAAD QHIAIRPGTD GALALAMAHV
     IIAEGLTDDD YIANHTVGYD EFAERVSRYT PEWAETETGV PADTIRTLAR EYAGAQPSVI
     RIGVAVERHA GGGQTVRALS CLPGLVGAWR KPGGGILQLP LWAFPVNWGA FMHPEMLTPG
     TRVINQYRLG AALAGDLPAG PPIKGLMVYN SNPVVTTPDQ DRLIKGLESE DLFTVVSEQF
     MTDTAEYADI VLPATTQLEQ DDIMFSWGHL YVTYNHQSIE PLGEAVPNTE MFRRLAAAMG
     FDDPVFQRTD EEMIAEAFDW SHPHMEGITV ESLKEQGWQR LNVAPPEAYA PHAEGNFPTP
     SGKAEFVSAA AAGGNFVVPL FRQGSNDHQP GQPVDPLPHY IPPRESAAAD PELAARYPLN
     LLTPKSHAFL NSSFASHEFH RRVANEHTLI VHPDDAAARG ITEGSPVRVF NDRGEFTVVA
     SLQDTVPLGV VVSPMGGWRK NSKAGATLAA VNPTVFGDLG NAPTFSDTLV EVETA
//
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