ID A0A2N5M8M9_9BACI Unreviewed; 678 AA.
AC A0A2N5M8M9;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:PLT30718.1};
GN ORFNames=CUU66_06060 {ECO:0000313|EMBL:PLT30718.1};
OS Peribacillus deserti.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX NCBI_TaxID=673318 {ECO:0000313|EMBL:PLT30718.1, ECO:0000313|Proteomes:UP000234748};
RN [1] {ECO:0000313|EMBL:PLT30718.1, ECO:0000313|Proteomes:UP000234748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V1-29 {ECO:0000313|EMBL:PLT30718.1,
RC ECO:0000313|Proteomes:UP000234748};
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:PLT30718.1}.
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DR EMBL; PGUY01000017; PLT30718.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5M8M9; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000234748; 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:UP000234748}.
FT DOMAIN 9..66
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 678 AA; 75616 MW; C9141663FA76F9D5 CRC64;
MASYVDEKNG VFPSVCSLDC PDQCGLLVYK ENGRIVRVEG DPNHPVTQGS ICNKVRNMPE
RLYDKKRLQF PLKRVGKKGS GQFERISWEE AIETITDKWK ALIQSYGAES ILPYSFYGNM
GNLTAEGMDR RFFNRLGASR LDRTICNSAG SAGYRYTMGG SIGTDPEETV HAKLIIFWGV
NAVSTNMHQI ALAQKARKNG AKIVVIDVHN NRTAKWADWF IPILPGTDTA LALGIMHILF
KENLTDPAFL KEFTVGSEEL KEHVVQYDPK SVSLITGVKV QDIYELARMY GKISPSFIRI
GNGPQHHDNG GMCIRTISCL PALTGQWLKK GGGAIKGNSA FLEHNSQALQ RPDLSAHNTR
IINMNLIGKA LHELDPPIRS LFIYGCNPAV VAPEGNKVRE GLLREDLFTV VHDLFLTETA
ALADIVLPAS SSFENTDFYT SYWHHYMQLQ QPVIEPWGES KSNVEVFRML AEGMNFTDSC
FKDSEEEMIR QALDFPGNPY LDSITFESLA ENQFVKADRE TLFPENLPTP SGKIELFSRK
MERDGYPPLP TYMPIPAENY PLLFVPAPNH NFLNSTFSNN EKHIKMEKTP QIFIHEDDAG
QRGIRDGDTV RIWNDRGECT LQASVGRDVL PGAVISLGLW ADLPGSSQLV NSLTPDRISD
MGGGAVFFSG RVDIEKAL
//
