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Database: UniProt
Entry: A0A5B8U5D5_9ACTN
LinkDB: A0A5B8U5D5_9ACTN
Original site: A0A5B8U5D5_9ACTN 
ID   A0A5B8U5D5_9ACTN        Unreviewed;      1083 AA.
AC   A0A5B8U5D5;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Molybdopterin-dependent oxidoreductase {ECO:0000313|EMBL:QEC48293.1};
GN   ORFNames=FSW04_12415 {ECO:0000313|EMBL:QEC48293.1};
OS   Baekduia soli.
OC   Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales;
OC   Baekduiaceae; Baekduia.
OX   NCBI_TaxID=496014 {ECO:0000313|EMBL:QEC48293.1, ECO:0000313|Proteomes:UP000321805};
RN   [1] {ECO:0000313|EMBL:QEC48293.1, ECO:0000313|Proteomes:UP000321805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BR7-21 {ECO:0000313|EMBL:QEC48293.1,
RC   ECO:0000313|Proteomes:UP000321805};
RX   PubMed=29299847; DOI=.1007/s12275-018-7107-6;
RA   An D.S., Siddiqi M.Z., Kim K.H., Yu H.S., Im W.T.;
RT   "Baekduia soli gen. nov., sp. nov., a novel bacterium isolated from the
RT   soil of Baekdu Mountain and proposal of a novel family name, Baekduiaceae
RT   fam. nov.";
RL   J. Microbiol. 56:24-29(2018).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR   EMBL; CP042430; QEC48293.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5B8U5D5; -.
DR   KEGG; bsol:FSW04_12415; -.
DR   OrthoDB; 9759518at2; -.
DR   Proteomes; UP000321805; Chromosome.
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; cd02792; MopB_CT_Formate-Dh-Na-like; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.30.200.210; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 2.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR048158; Formate_DH_Act.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   NCBIfam; NF041513; formate_DH_Act; 1.
DR   PANTHER; PTHR43598:SF1; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT; 1.
DR   PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 2.
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   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
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:UP000321805}.
FT   DOMAIN          42..98
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
FT   REGION          340..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          887..915
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1083 AA;  119297 MW;  32C88B8B9429444C CRC64;
     MTGPVRGWPV LRQALGRDRT ARGAAAKSAA TSRLQPRTTT ADRVVKSICP YCAVGCGQDV
     YVKDDKVVQI EGDPDSPVSR GRLCPKGSAS LQLTTGAARE HHVLYRRPHG TDWEALDLDT
     AMDMIADRVL SARREGWQWT VEGKDVRRTM GLATLGGATL DNEENYLIKK LMTALGVIQV
     ENQARVCHSS TVAALGTSFG RGGATTFPRD LTNSDCIVIQ GSNMAEAHPV AFQWVTEAKA
     RGATIIHVDP RFSRTTALAD FHVPTRAGTD IAFLGGIINH VLTEGRHFRE YVEAYTNAAA
     IIDEDFQDTE DLDGLFSGFQ PETHSYDYTS WQYDGALVQA ASGERDSDPA ASQRRESVTS
     SGHGESHGSG GHDVPDPKTD PTLQDPRCVW QILKRHYARY TPEMVERTCG VPQPLFRRVC
     DAVCDNSGRD RTTAFVYAVG WTQHTAGVQY IRAASILQLL LGNIGRPGGG IMAMRGHASI
     QGSSDIPTLY DLLPGYLPMP HAHEHEDLDT YVQADEARKG FWGNMGSYTV SLLKAWFGDA
     ATRDNDFCFG LLPRLTGGHS TYDTVIEQLE GRCKGYMLLG ENPAVGSANV RLQRQGMANL
     DWLVVRDFSL IESATWWKDG PEVESGELRT EDNATEVFFL PAASHTEKSG TFTNTQRLLQ
     WHHAAVEPAG DARSDLWFMY HLGRRIREKL AGSNDPIDEP VLALTWDYPT HGPLAEPSAE
     AILAEINGYD GDGRPISSYT QLANDGSTSC GCWIYAGVYA DGVNQAARRK PVGEQDWIAP
     EWGWAWPANR RILYNRASAD PDGAPWSARK ALLRWDEEEG TWTGPDVPDF EADKRPDYRP
     AEDAVGPAAI AGDEPFIMQA DGRGWLYVPA GLTDGPLPAH YEAQDSPVQN PLYGQQRNPV
     RKTYPRKGNR YHPSGDEPGA GVFPYIITTY RLTEHFTAGG MSRWTPYLAE LQPEMFCEVS
     PELAGERDLV HGDWATVITA RGAVEARVLV TQRMRPLEIG GPPARTIHTI GMPWHWGPNG
     YSRGDAMNEL TAISLDPNVH IQEDKALTAD IRPGRRPRGA ERRELVDDYI RRAGIDDQTG
     SRP
//
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