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Database: UniProt
Entry: A0A418X428_9BURK
LinkDB: A0A418X428_9BURK
Original site: A0A418X428_9BURK 
ID   A0A418X428_9BURK        Unreviewed;       699 AA.
AC   A0A418X428;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Molybdopterin oxidoreductase family protein {ECO:0000313|EMBL:RJG07189.1};
GN   ORFNames=D3870_15320 {ECO:0000313|EMBL:RJG07189.1};
OS   Noviherbaspirillum cavernae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Noviherbaspirillum.
OX   NCBI_TaxID=2320862 {ECO:0000313|EMBL:RJG07189.1, ECO:0000313|Proteomes:UP000285190};
RN   [1] {ECO:0000313|EMBL:RJG07189.1, ECO:0000313|Proteomes:UP000285190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K2R10-39 {ECO:0000313|EMBL:RJG07189.1,
RC   ECO:0000313|Proteomes:UP000285190};
RA   Zhu H.;
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:RJG07189.1}.
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DR   EMBL; QYUN01000002; RJG07189.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A418X428; -.
DR   OrthoDB; 9815647at2; -.
DR   Proteomes; UP000285190; 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; 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:UP000285190}.
FT   DOMAIN          3..60
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   699 AA;  76907 MW;  29F426CD257F27DA CRC64;
     MTTSIVRAAC PHDCPDTCAM LVTVQDGVAT EVRGDPEHPP TAGALCTKVS RYVERTYHKD
     RLLHPLKRIG RKGEGRFERI SWDEALTTIS SRLQSIAARD PQAILPYSYA GTMGLVQGES
     MAARFFHKLG ASFLDRTICA TAGGVGYRYT IGARIGTDLE QFQNAKLILI WGGNPIASSV
     HFWMRAQEAK RRGAKLIAID PYRSLTAEKC HQHIALLPGT DAALALGMMH VLIAEHLLDE
     DYIARHTLGF EQLKERVREW TPERTAQTCG ITAQEVQQLA REYGTTAKGG DAVAIRVNYG
     VQRVRGGGMA VRNIACLPAL VGAWRHAAGG VQLSVSDTFP KNNQALQRPD LLPVGAAPRT
     INMSTIGDDL LREASPEFGS KIEAVIVYNS NPVAVAPESS KVAQGFARED LFTVVLEHFQ
     TDTADYADIV LPATTQLEHV DIHSTYGHLY MMANNAAIAP LGEAKPNTEI FRLLAARMGF
     DDACFKESDD EIAAQAFNKN DVRAIHFDWH ALKQKGWQKL NVPDAPFAEG GFPTPSGKCE
     FYCARMQADG LDPLPTYIPP YESVASNPEL AKRYPLAMIS PPARNFLNST FVNVQSLRNT
     EGEPHLDIHP IDAARRTIEN GARVRIYNER GAFVAKARVT DKTRQGLVVG LSIWWKKLAA
     DGRNANEVTS QRLTDMGAAP TFYDVLVEVE RVDHRSIAR
//
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