(data stored in SCRATCH zone)

SWISSPROT: A8FQ40_SHESH

ID   A8FQ40_SHESH            Unreviewed;       809 AA.
AC   A8FQ40;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   08-MAY-2019, entry version 83.
DE   SubName: Full=Anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family protein {ECO:0000313|EMBL:ABV34963.1};
GN   OrderedLocusNames=Ssed_0350 {ECO:0000313|EMBL:ABV34963.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34963.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34963.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34963.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539;
CC         Evidence={ECO:0000256|SAAS:SAAS00648551};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|SAAS:SAAS00607242};
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|SAAS:SAAS01108232}.
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DR   EMBL; CP000821; ABV34963.1; -; Genomic_DNA.
DR   RefSeq; WP_012140701.1; NC_009831.1.
DR   STRING; 425104.Ssed_0350; -.
DR   EnsemblBacteria; ABV34963; ABV34963; Ssed_0350.
DR   KEGG; sse:Ssed_0350; -.
DR   eggNOG; ENOG4108J2R; Bacteria.
DR   eggNOG; COG0243; LUCA.
DR   HOGENOM; HOG000284390; -.
DR   KO; K07306; -.
DR   OMA; FGFHYKA; -.
DR   OrthoDB; 88184at2; -.
DR   BioCyc; SSED425104:G1G9Y-366-MONOMER; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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   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; IPR027467; MopterinOxRdtase_cofactor_BS.
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; SSF50692; 1.
DR   TIGRFAMs; TIGR02166; dmsA_ynfE; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FQ40.
DR   SWISS-2DPAGE; A8FQ40.
KW   4Fe-4S {ECO:0000256|SAAS:SAAS00418020};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Iron {ECO:0000256|SAAS:SAAS00454562};
KW   Iron-sulfur {ECO:0000256|SAAS:SAAS00454505};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00077323};
KW   Oxidoreductase {ECO:0000256|SAAS:SAAS01133048};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002015}.
FT   DOMAIN       41    102       4Fe-4S Mo/W bis-MGD-type.
FT                                {ECO:0000259|PROSITE:PS51669}.
SQ   SEQUENCE   809 AA;  89135 MW;  DF83D66FED831D8A CRC64;
     MERRSFLKMS AALSCAATVS GCNSSSKDVE VVPPTPPVAG ENLNWSACLV NCGSNCPVQV
     FSTDGVITRV ESEFTTTDKY GDHDVRACLR GRSLRKRVYA PDRLKYPMKR VGPRGSGQFE
     RISWDEALDL VAEKLQGTID QYGNESIHFT YNSGARYHFS GKQCLYRLMN LKGGYLNAYG
     DYSWSQIYEA AGQTYGSAGP GWQGSSVSEM QNSDLVLMVG YNPSEIRMSG SGEAYDFLMQ
     KQKNKFKTIL IDPRYTDSAV GKEDQWLAIR PGTDAALFEA LAYEWITTNT VDQAFLDKYC
     VGYDEKTMPA GVGYEESYKA YILDNTTVGS SIPGVNAKTP EWAAAITGIE AHIIVELARE
     LAAARAPFIQ IAASLNRQAA GENNTRAGYM LPILLGQLGL PGTNCGGLCK GSFLHAPFMP
     TGSNPVKKAI SFFTFTQAIE DGKNMTVLSD GVQGVDTDEE GDGKLGTDIK AIINYGGNAL
     INQHSDVRKT EKLLQDESKC EFILVVDNWM TPSAKFADVL LPDVTWLESE DLIYQSYAAG
     DTATLVQMSS GVDPMFESRP IYEVCVDLAK RMGVEAEFTE GKSRKDWLDQ FYAESKAATP
     GLPDKEVMLT QGIYRKYLPD GGYIVLEDFR NDPEANPLGT PSGKIEIYSS RLADKARTWK
     LKEGDVISAL PKYVPTWEGY EDTETKKKYP LQLTGYHTKG RAHSSYHNVP WLREVVQDAV
     WMNPLDANKR GLKTGDKVHI FNDRGTIEVE VKVTPRIMVG VTALGQGAWF QPGGDVDKGG
     CLNVLTTQRT TPVTKGNPQH TNLVEIRKV
//

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