ID A0A098EZX7_9BACI Unreviewed; 791 AA.
AC A0A098EZX7;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:CEG26947.1};
GN ORFNames=BN1002_01801 {ECO:0000313|EMBL:CEG26947.1};
OS Bacillus sp. B-jedd.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1476857 {ECO:0000313|EMBL:CEG26947.1, ECO:0000313|Proteomes:UP000042335};
RN [1] {ECO:0000313|EMBL:CEG26947.1, ECO:0000313|Proteomes:UP000042335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-jedd {ECO:0000313|EMBL:CEG26947.1,
RC ECO:0000313|Proteomes:UP000042335};
RA Urmite Genomes Urmite Genomes;
RL Submitted (SEP-2014) 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}.
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DR EMBL; CCXR01000001; CEG26947.1; -; Genomic_DNA.
DR RefSeq; WP_048824597.1; NZ_CCXR01000001.1.
DR AlphaFoldDB; A0A098EZX7; -.
DR STRING; 1476857.BN1002_01801; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000042335; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0009389; F:dimethyl sulfoxide reductase activity; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR CDD; cd02770; MopB_DmsA-EC; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.12440; -; 2.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR011888; Anaer_DMSO_reductase.
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; IPR006311; TAT_signal.
DR NCBIfam; TIGR02166; dmsA_ynfE; 1.
DR PANTHER; PTHR43742:SF3; DIMETHYL SULFOXIDE REDUCTASE DMSA; 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; PS51318; TAT; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000042335};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 54..115
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 791 AA; 88433 MW; 8B4C2450AED98AA4 CRC64;
MTEKNSQGNK LSRRSFLKWT GALSVPVVAS GVVSAKYLKK NTSVAKVKSS PIPEKIIPTC
STFDCGGKCM VKAHVKDGVI VRVSARASGE LDEQNPFMKA CVRGRSYRKY QYHPDRLKYP
MKRTGKRGEG KFERISWEEA IDIITSETKR ITDKYGPESR YVHQGTAVTG GSMGGAALAR
RLFSLNGGHL SYYHSVSMGN TAAATPYTYG THQTGSSLDS LEHTNLVILW GHNPSETIFG
NTNHYYLKLK KKGVKFISVD PRYSDTAAAF ADEWIPLLPG TDNALMDAMA YVIVKENLHD
KEFLQKYVVG FDEEHMPEGV PANESLTSYL FGKKDGLEKT PEWAEKITKV PAEKIRGLAR
EYANAKPAAL IQGWGPQRHA SGERIARGGT MLAVITGNVG KAGGWASGYG GIQRKFPVDV
PEPENPFKGS ISIMSWTEAI TDAASITPAE GLKGVDKLTT NVKLIYNLAG NYLVNQQPDI
NKTIKILEDE NLVEFIVVSD HFLTPSAKYA DILLPETTFF ERWNLGGSWA SGDYFILSEK
VVENFYEARS DYEWLSEVAK GLGVGVEFTE GRDEVGWIKY ILDETRKVEP DTPTFEELKK
KRIHYWRYDG PRIAFKEQID DPENNKFETP SGKIELFSNL LYEMKNPEIP AIPSYVPEWE
GAEDPLKEKF PLQCITWKGK NRMNSSFFNH PWQQQVAKQK LWINPIDAEV RKLKQGDSFR
VFNDRGTMVI PVEVTPRIIP GVVAMQAGAW YKPDEKGIDH GGCPNVLTSQ RRTPLANGNA
HQTMLVEVTK A
//