ID   A0A172S027_9ACTN        Unreviewed;       803 AA.
AC   A0A172S027;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Tat-targeted selenate reductase subunit YnfE {ECO:0000313|EMBL:SEO37920.1};
GN   ORFNames=SAMN02910314_00050 {ECO:0000313|EMBL:SEO37920.1};
OS   Denitrobacterium detoxificans.
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Denitrobacterium.
OX   NCBI_TaxID=79604 {ECO:0000313|EMBL:SEO37920.1, ECO:0000313|Proteomes:UP000182975};
RN   [1] {ECO:0000313|Proteomes:UP000182975}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21843 {ECO:0000313|Proteomes:UP000182975};
RA   Varghese N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR   EMBL; FOEC01000001; SEO37920.1; -; Genomic_DNA.
DR   RefSeq; WP_066664297.1; NZ_FOEC01000001.1.
DR   AlphaFoldDB; A0A172S027; -.
DR   STRING; 79604.AAY81_09265; -.
DR   KEGG; ddt:AAY81_09265; -.
DR   PATRIC; fig|79604.3.peg.1860; -.
DR   OrthoDB; 7376058at2; -.
DR   Proteomes; UP000182975; 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   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.12440; -; 2.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 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   InterPro; IPR019546; TAT_signal_bac_arc.
DR   NCBIfam; TIGR02166; dmsA_ynfE; 1.
DR   NCBIfam; TIGR01409; TAT_signal_seq; 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:UP000182975};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..803
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039694458"
FT   DOMAIN          47..108
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   803 AA;  88184 MW;  3268844677562E92 CRC64;
     MNDVTMNRRS FVKTAGALGA LAAAGGAISA EGSLFGESSI AHADTEEQTV WQHCGVNCGG
     ACALQCHVKD GSIEYVESDN TGSSDMNSVQ VRACLRGRSI RRWLQSPDRL NYPMKRVAGT
     KRGEGKYERI SWDEALDTIA SEMKRIRSTY GDTAMYIHYA SGVSSGIIAG TPVNRLFNLT
     GGYLKTYGSY SSAQISAAGT YTYGGGTYGS SFLTLQDNEL VVMFGNSPAD TRMGGGGHTW
     DFARMREAKN LRVICIDPRM SDTVCGQGGE WIPIVPGTDG ALCAALAYQW ITNDQVDTEF
     LHKYCVGYDE ETLPEDAKGK NASYKDYILG NGADKTAKTP AWASAITKIP EQRIIELADE
     MAKADPVYIC QGYGVERHSN GENAARCIMV LPQLLGQIGK PGTNDGRREG CNSIQAIATF
     PAGKNPVPDT ISLYTWPDAI DHGEQMTATN AGVQGVEKLS NSIKFLFNYG GNALTNQHSD
     INATHELLQD ESKCEFIVTS EVFMTDSAKY SDIILPDLAV QEQLDISKGG YADNDEVLFF
     CDPVYEPVGE RRGIYEVCTD LAERLGVKDQ FTEGKTREEW LRSLYEQARE KDSTLPTWEE
     GFKMGVYKRD TKPKLSLEKF VADPEANPLP TESGKIQIYS EKLAKFAQTW ELNDGDKITA
     LPEFDPAFDS YLDVSEEYPL LLMGFHYKAH VHSSYSNNSV LQTAALHQLW INPEDAQTRG
     ISTGDMVSVK TERGEVRIMA KVTNRVIPGT VVMPQGMWHD ADMDGDRIDK GGCINTLTRY
     RPTALAKANP QHSNVAQVEK VSE
//