ID E3E787_PAEPS Unreviewed; 710 AA.
AC E3E787;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 2.
DT 24-JAN-2024, entry version 73.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:ADO58942.2};
GN Name=yoaE {ECO:0000313|EMBL:ADO58942.2};
GN ORFNames=PPSC2_23475 {ECO:0000313|EMBL:ADO58942.2};
OS Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO58942.2, ECO:0000313|Proteomes:UP000006868};
RN [1] {ECO:0000313|EMBL:ADO58942.2, ECO:0000313|Proteomes:UP000006868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:ADO58942.2,
RC ECO:0000313|Proteomes:UP000006868};
RX PubMed=21037012; DOI=10.1128/JB.01234-10;
RA Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT activity.";
RL J. Bacteriol. 193:311-312(2011).
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}.
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DR EMBL; CP002213; ADO58942.2; -; Genomic_DNA.
DR RefSeq; WP_016324832.1; NC_014622.2.
DR AlphaFoldDB; E3E787; -.
DR STRING; 1406.LK13_10965; -.
DR KEGG; ppm:PPSC2_23475; -.
DR PATRIC; fig|886882.15.peg.4969; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_9; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000006868; 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; IPR006655; Mopterin_OxRdtase_prok_CS.
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.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 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:UP000006868}.
FT DOMAIN 28..85
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 710 AA; 79167 MW; 652BB3C67350CB3F CRC64;
MDHRNSAPLE ATLQHNLHRG QRMTEQQNGI FPAVCPLDCP DTCGLLLHKE NGKIVKVTGN
PDHPITKGAI CNKVRNMTER VYDPDRVLYP LKRVGAKGEG KFERISWEEA VDTITGRFKE
LIRTDGPESI LPYSFYGNMG VLSVDGMDRR FFNALGSSQL DQTICSVAGN EGWASVMGFK
GGTSPEDTED AELIIVWGGN VISTNMHQVV LAEKARKKGA KVVVIDVHRN RTAQWADWFI
PLYPGTDTAL ALGVMHVLFD QGLTDDEFLR RYTVGHEELR EHVKTYTPER VSQITGVPKE
DIIRLAEMYG KARAAYINIG NGLQHHDNGG MNVRAVTCLP ALTGQWLKHG GGASRSNGAY
AKINSAHLER PDLRQNPDAR VINMNRIGEA LLQKEQPIKA LFVYCSNPVV VAPDSERVTE
GFEREDLFTV VHDLFLTDTA CYADIVLPAA SSFEGTDLYK SYWHHYIQMQ KPVIDPLGES
KSNYELFSLL GQAMGFDEAA FTESEEDMIA GALDNPTNPY LNGVTLDALK KSPFVKLDMT
PKATYLERLT TPSGKIELYS EKMKQAGLPA LPSYVPLIEG YDGEHRPQAD DRFPLMFVSP
PNHNFLNSTF ANLPKHQRLE REPLLQIHPE DAQARDIADG DPVTVWNDRG MYELKAKVTD
LMLPGTVISQ GLWWKGKGRR QRANALTSDR LSDMGQGATF FSTVVNVKRQ
//
