ID A0A2N5MF15_9BACI Unreviewed; 684 AA.
AC A0A2N5MF15;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:PLT32952.1};
GN ORFNames=CUU64_16075 {ECO:0000313|EMBL:PLT32952.1};
OS Bacillus sp. V5-8f.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2053044 {ECO:0000313|EMBL:PLT32952.1, ECO:0000313|Proteomes:UP000235260};
RN [1] {ECO:0000313|EMBL:PLT32952.1, ECO:0000313|Proteomes:UP000235260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V5-8f {ECO:0000313|EMBL:PLT32952.1,
RC ECO:0000313|Proteomes:UP000235260};
RA Seuylemezian A., Cooper K., Vaishampayan P.;
RT "Comparitive Functional Genomics of Dry Heat Resistant Strains Isolated
RT from the Viking Spacecraft.";
RL Submitted (NOV-2017) 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:PLT32952.1}.
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DR EMBL; PGUW01000017; PLT32952.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5MF15; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000235260; 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.
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:UP000235260}.
FT DOMAIN 9..66
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 684 AA; 75702 MW; C2ACB8683353F011 CRC64;
MESYINQPDG IFPSVCSLDC PDQCGLLLHK KDGKIIKVEG DPTHPVTKGN ICNKVRNMTA
RLYDPKRLKY PLKRVGAKGE GKFERITWKE AIETITSKWK DLIELHGPQS ILPYSFYGNM
GNLSAEGMDR RFFNRMGASR LERTICNAAG STGYKYTMGG SFGTDPEETA HSKLFIFWGI
NAVSTNMHQV TIAQQARKNG AKIVVIDVHK NQTGRWADWF IPILPGTDAA LALGIMHVLF
AENMQDEEFL KQYTVGAEEL KQRAAQYDPA TVSAITGVSV DDIYKLARMY GTISPSYIRI
GNGLQHHDNG GMCVRTISCL PAITGQWLIK GGGATKGNSG YLAYNTRALQ RPDLLKDKST
RIINMNAIGK ALLELEEPIR SMFVYNSNPA IIAPDANKVR MGLMREDLFT VVHDLFLTET
AAYADIVLPA AASFETTDFY ASYWHHYMQI QLPVVETYGE SKSNTEVFRL LAAEMGYDEE
VFKATDEQLI EEALDHPANP YLEGISLKGL LERQYLKASV KPIVSGSLPT PSGKIELYSE
QMFKDGFDPI PVYHPIVEDG DLPFLFVPAP NHNFLNSTFS NNARHIALEK EPRLHMNASD
AAKISIEDGD MVRIHNHRGE CVLKAAVGEN VLPGVLVSQG LWADTPGTKQ LVNALTPDRI
SDMGGGATFF SGRVDAEKII VPKG
//
