ID   A0A4R1PVK1_9FIRM        Unreviewed;       792 AA.
AC   A0A4R1PVK1;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Anaerobic dimethyl sulfoxide reductase subunit A {ECO:0000313|EMBL:TCL36220.1};
GN   ORFNames=EV210_109169 {ECO:0000313|EMBL:TCL36220.1};
OS   Anaerospora hongkongensis.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Anaerospora.
OX   NCBI_TaxID=244830 {ECO:0000313|EMBL:TCL36220.1, ECO:0000313|Proteomes:UP000295063};
RN   [1] {ECO:0000313|EMBL:TCL36220.1, ECO:0000313|Proteomes:UP000295063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15969 {ECO:0000313|EMBL:TCL36220.1,
RC   ECO:0000313|Proteomes:UP000295063};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (MAR-2019) 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:TCL36220.1}.
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DR   EMBL; SLUI01000009; TCL36220.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4R1PVK1; -.
DR   OrthoDB; 219031at2; -.
DR   Proteomes; UP000295063; 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; 1.
DR   Gene3D; 3.30.2070.10; Formate dehydrogenase/DMSO reductase; 1.
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; 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; 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:UP000295063};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          53..114
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   792 AA;  88039 MW;  AC6A446C7E57782C CRC64;
     MSEKENQGPF SLTRRRFLAW SAAVAGSSSL LHWAEAANSF EPVTAGATVQ RNEKVVLTSG
     SHNCGGRCQI KAHVKDGVIV RITTDDKITD SEAVPQLRGC LRCRSYRNRL YHTDRLKYPM
     KRVGKRGEGK FVRITWEEAI TTIADHTRRI MAQYGPEAIF LHYASGIAGK VAERVWMGRL
     LGLYGGYLSY YGTYSTACTQ AATPYTYGTV ATGNSREDWV NSKLIILLGF NPAETVHGTN
     TPYYLKLAKE AGAKIVVIDP IYSSTAIALA DEWIPIKPTT DNALLDAMAY VMITENLHDQ
     AFLNKYCLGF DEEHMPPGIP AGQSYKSHVL GQGGDDTAKT PEWAEAITGV PRDTIIRLAR
     EYAQLRPGAL IQGYGPQRHA YGEQVVRGGT VLAAMTGNVG VKGGWASGTG YKARDQVVGS
     IPSQNPCKAS ISCFIWPDAI QRGKEMGAAD GVRGVPKLSS NIKMIYNLAG NCLINQHSDC
     NGTAKLLADE SLVECIVVSE HFMTASAKFA DILLPSDNYM ERDDIVSPWG WGDYLLYMNK
     AVDTVFECRN GYDWISELAE QLGIKEKFTE GKSKEDWLRY LVDKTRQANP GFPTWEEFKE
     QGVYRWKYDK PSIAFQKQIE EPDKYKFSTP SGKIEIFSPR LWAMNKPELI PAVPKYIPAW
     EGPQAPLARQ YPLQCIGHHY KRRVHSTFDN VPWLEEASAQ EVWMNPADAA ERGLKAGDKV
     KVFNDRGVMV IPVKITSRIM PGVVSVPQGA WWTPDENGID RRGCTNTITK YHPTPLAFGN
     PQHTNLVQIA KN
//