ID A0A371J8Y0_9FIRM Unreviewed; 666 AA.
AC A0A371J8Y0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:RDY29211.1};
GN ORFNames=CHL78_002575 {ECO:0000313|EMBL:RDY29211.1};
OS Romboutsia weinsteinii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Romboutsia.
OX NCBI_TaxID=2020949 {ECO:0000313|EMBL:RDY29211.1, ECO:0000313|Proteomes:UP000215694};
RN [1] {ECO:0000313|EMBL:RDY29211.1, ECO:0000313|Proteomes:UP000215694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCRI-19649 {ECO:0000313|EMBL:RDY29211.1,
RC ECO:0000313|Proteomes:UP000215694};
RX PubMed=28982987;
RA Maheux A.F., Boudreau D.K., Berube E., Boissinot M., Cantin P., Raymond F.,
RA Corbeil J., Omar R.F., Bergeron M.G.;
RT "Draft Genome Sequence of Romboutsia weinsteinii sp. nov. Strain CCRI-
RT 19649(T) Isolated from Surface Water.";
RL Genome Announc. 5:e00901-17(2017).
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:RDY29211.1}.
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DR EMBL; NOJY02000003; RDY29211.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371J8Y0; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000215694; 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 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 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:UP000215694}.
FT DOMAIN 5..63
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 666 AA; 76079 MW; 3BA5EB2AB47D0419 CRC64;
MDSDIKKLSH GCTLDCFDAC KFNVYVDDNK NIIKIEGDKE HPYTKGIICS KGRAHLDRLN
HENRIYTPLL KVDGKWIEIS FEEAIDIMAK KLNYYKEEYS SKSVMYYEQY GNGSVLKSIG
DIFFNFYGGA SKQKGGPCWS AGIKAQTYDF GDVKGHALED MLNSKSIFIW GKNPAYTTIH
TMQILKKAQQ KGSKVIVIDP ICTSTAKIAD KYIRIKPGTD GALAMAMAKI IIKEKLHDEE
YINNYVLGFE EYKEYIDTLE LDYLIEECGI DLDDIRELVN LYTDKYCTIH LGYGMQKYKN
GGNTIRAIDA LGAITGQVGF SGGGVNYANR VYPNILNSDP YKSLDYGNNR EFYVSKISKF
IKNPNDNCVG EGDNIPIKMA VVVKSNLLAQ LPNLVELEDA FSKIEFKVCI DMFMTDTASA
CDLFIPATNT LESEDILYSS MTNPYITYNE KIVEPKNKLM DEYYFFAELA KVMGIKNYPI
VDKREYLSKV IEPLKEFNEI ISLEWIANNY FTIHKPVAWD DKKFDTPSGK YELYSRQVEY
LGISPIPVYI SGKKENKFRL LTNHHRDTLF SQHYMDKKGI SQAYINKKMA INLNVENKEV
VSLKCKQFNI DVEINIDDSV SDYVVKMYVG WWKKHGNPNF ITDSGISDIG GQITYNETFV
DIIKQK
//
