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Database: UniProt
Entry: D6Y952_THEBD
LinkDB: D6Y952_THEBD
Original site: D6Y952_THEBD 
ID   D6Y952_THEBD            Unreviewed;       673 AA.
AC   D6Y952;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:ADG90014.1};
GN   OrderedLocusNames=Tbis_3324 {ECO:0000313|EMBL:ADG90014.1};
OS   Thermobispora bispora (strain ATCC 19993 / DSM 43833 / CBS 139.67 / JCM
OS   10125 / KCTC 9307 / NBRC 14880 / R51).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Thermobispora.
OX   NCBI_TaxID=469371 {ECO:0000313|EMBL:ADG90014.1, ECO:0000313|Proteomes:UP000006640};
RN   [1] {ECO:0000313|EMBL:ADG90014.1, ECO:0000313|Proteomes:UP000006640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19993 / DSM 43833 / CBS 139.67 / JCM 10125 / KCTC 9307 /
RC   NBRC 14880 / R51 {ECO:0000313|Proteomes:UP000006640};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Mikhailova N., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F.,
RA   Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA   Wu D., Jando M., Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Thermobispora bispora DSM 43833.";
RL   Submitted (JAN-2010) 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; CP001874; ADG90014.1; -; Genomic_DNA.
DR   RefSeq; WP_013133547.1; NC_014165.1.
DR   AlphaFoldDB; D6Y952; -.
DR   STRING; 469371.Tbis_3324; -.
DR   KEGG; tbi:Tbis_3324; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_13_3_11; -.
DR   OrthoDB; 7376058at2; -.
DR   Proteomes; UP000006640; 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: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:UP000006640}.
FT   DOMAIN          2..59
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   673 AA;  73736 MW;  C3099A6DF16E8752 CRC64;
     MTSTTFGACP LDCPDTCSWV VTVQDGKAVS LRGNREHPFT RGALCVKVNR YLEHARAADR
     ILYPMRRVGP KGSGRFERIS WDEALSEIAT RLHSIIDEYG GEAIWPYQGT GTLGYIQGES
     GKAGRRFWNV LGASKHDMNI CSRAGNVGLR YVNGTPGGMD PETFALSKLI LLWGTNPLTS
     GHHVWKFIQE ARAAGAYVVA IDPIRTRTAD QADEHLPIRP GTDAALALGL LHVVLEEGAE
     DRDFIERYTL GWEEFQAEIR KYPVDRVAEI TGLPAERIRS LGVRLAHTRP TGIRVTMGIQ
     RHAGGGAALR AIACIPGVTG DWRYPGGGLV YSTSAHARLN VDVREDLLPK PVRTLTMTRL
     ASSLDETVKC LWVYGANPVG SSPDQNRIRA ALQREDLFTV VMEHFPTDTV DYADIVLPAT
     MQIEHMDLHA GYGHMYLIWN EPAVEPPGEC LSTTETFRRL ARHMGLTEPC LYDSDLEIAE
     QLLSTTGISL EELRKKGWAR LDVPDPFLPF ADGFPTPSGR LEFVSARAEA DGQPRVPGYT
     PSLTAGTAPA DRAYPLTLIT PAQHMFLNTT FGNNPELLRR SKGPKVLVNE ADAKPRGLVD
     GQLARVFNRN GEFTAYVEIT DRVRPGVVAA PKGHWPKLSP GGANPNAVVD ERDADMGKGA
     VFHDNFVDIA PAG
//
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