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Database: UniProt
Entry: A0A438MIT9_9ACTN
LinkDB: A0A438MIT9_9ACTN
Original site: A0A438MIT9_9ACTN 
ID   A0A438MIT9_9ACTN        Unreviewed;       667 AA.
AC   A0A438MIT9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Anaerobic selenocysteine-containing dehydrogenase {ECO:0000313|EMBL:RVX45375.1};
GN   ORFNames=EDD27_8168 {ECO:0000313|EMBL:RVX45375.1};
OS   Nonomuraea polychroma.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Nonomuraea.
OX   NCBI_TaxID=46176 {ECO:0000313|EMBL:RVX45375.1, ECO:0000313|Proteomes:UP000284824};
RN   [1] {ECO:0000313|EMBL:RVX45375.1, ECO:0000313|Proteomes:UP000284824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43925 {ECO:0000313|EMBL:RVX45375.1,
RC   ECO:0000313|Proteomes:UP000284824};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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:RVX45375.1}.
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DR   EMBL; SAUN01000001; RVX45375.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A438MIT9; -.
DR   OrthoDB; 7376058at2; -.
DR   Proteomes; UP000284824; 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:InterPro.
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; 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.
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   Reference proteome {ECO:0000313|Proteomes:UP000284824}.
FT   DOMAIN          4..61
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   667 AA;  72341 MW;  97DA787200C0DB82 CRC64;
     MSGELKVLGA CPLDCPDTCS WIVTVDDGKA VKLRGNPDHP YTRGALCVKV NRYLEHTQAA
     DRILHPLRRT GPKGSGQFER ITWEEALEEI SVRLRAIVEE HGGEAIWPYL GTGTLGYLQG
     CEGVAGRRFW NVLGASKHFL NICAAAGGSG LHRTNGTPAG MDPENLALAK LILLWGTNTL
     TSGHHLWKFI QDARANGAHV VAIDPIRTRT ADQADEYLPI RPGTDAALAL GLLNVVLAEN
     AQDEEFLAEH SEGWPEFREE ILRHPVGKVS EITGIPAADI HSLGMKLAHT RPTAIRATMG
     IQRHAGGGTA LRTIGAIPGV TGDWRHPGGG IAYSTSGHVH LDIDTREDLL AKPVRTLVMT
     KLASQLDDVK CLWVYAANPL GSTPDGNAIR RQLAREDLFT VVMEQFPTDT VDYADIVLPA
     TMQTEHYDLH AGYGHMYLLW NEPAVEPAGE CLSTTETFRR LAAHMGLTEP SLYDSDLELA
     EQLLSSGHPS LEGITLDRLR KEGWVRMNYP KPFIPFADGF PTPSGRLRFP RAGQAYIPPH
     TAQAERSPYP LALVTPAAHT FLNTIFGNNP ELRRRAKDPV VLVNPADAAA RGLVSGQRVR
     VHNDGGEFLA DVEISDRVAA GVVASPKGRW PKLSPGGANP NAVVAERDAD MGKGPGYHDN
     LVEVSPA
//
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