(data stored in ACNUC7421 zone)

SWISSPROT: A8FQ49_SHESH

ID   A8FQ49_SHESH            Unreviewed;       816 AA.
AC   A8FQ49;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 72.
DE   SubName: Full=Anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family protein {ECO:0000313|EMBL:ABV34972.1};
GN   OrderedLocusNames=Ssed_0359 {ECO:0000313|EMBL:ABV34972.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34972.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34972.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34972.1,
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:SAAS00637151};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|SAAS:SAAS00637177};
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|SAAS:SAAS00648863}.
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DR   EMBL; CP000821; ABV34972.1; -; Genomic_DNA.
DR   RefSeq; WP_012140710.1; NC_009831.1.
DR   ProteinModelPortal; A8FQ49; -.
DR   STRING; 425104.Ssed_0359; -.
DR   EnsemblBacteria; ABV34972; ABV34972; Ssed_0359.
DR   KEGG; sse:Ssed_0359; -.
DR   eggNOG; COG0243; LUCA.
DR   HOGENOM; HOG000284390; -.
DR   OMA; CAKGYAY; -.
DR   OrthoDB; POG091H04DN; -.
DR   BioCyc; SSED425104:GH7Q-368-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   InterPro; IPR011888; Anaer_DMSO_reductase.
DR   InterPro; IPR009010; Asp_de-COase-like_dom.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   Pfam; PF10518; TAT_signal; 1.
DR   SMART; SM00926; Molybdop_Fe4S4; 1.
DR   SUPFAM; SSF50692; SSF50692; 1.
DR   TIGRFAMs; TIGR02166; dmsA_ynfE; 1.
DR   TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FQ49.
DR   SWISS-2DPAGE; A8FQ49.
KW   4Fe-4S {ECO:0000256|SAAS:SAAS00657262};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Iron {ECO:0000256|SAAS:SAAS00509295};
KW   Iron-sulfur {ECO:0000256|SAAS:SAAS00077451};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00509306};
KW   Molybdenum {ECO:0000256|SAAS:SAAS00648831};
KW   Oxidoreductase {ECO:0000256|SAAS:SAAS00509324}.
FT   DOMAIN       44    107       4Fe-4S Mo/W bis-MGD-type.
FT                                {ECO:0000259|PROSITE:PS51669}.
SQ   SEQUENCE   816 AA;  89589 MW;  BC3E3B17D9052E6E CRC64;
     MERRTFLKFS AAAAAVATVT GCESSSASNP LPAPSEPVLP PVGEGITWGS CATNCWQACP
     LKVHSKDGVI TRIETEGKAT DDWDNFDHEI RPCPRGRSMR QKVYNHDRLK YPMKRVGRRG
     SDEFVRISWE EAVSSVASAM EQTYSQYGKN AIFMPLGGGS HDLNTGVTQS SVRLLNMAGG
     CLFFHNDYSA AQYREGSAGM YGYLASNAGD TVGFWNTGSS LRSLEDSDLM VCFGYNPMEA
     RLGGAGSGYE YLNVKKKNNF KTYYIDPRFT DTAVTANDEW IPIRPGTDAA LCEAIAYVLI
     EDGYADIPFL EQYTHGYDKY QDYITGVTDG TTKTPERAEG ICGIPAEKIR EIAQAIGAAS
     APFVTQGFGP QRQGNGENNA RAVMMLPLLV GKISGDGTNH GGTPGNDGLS HYAMMPADTL
     QDLMNMKIMD VTIPAASHLD AIEFGMQMKP STHDVRYSNP DLMAADTPLE TNVRFLWLAS
     SNMLANQNGD INRADRLLND ESLVDFVVVV EQHMTASAKY ADIILPEVSW LEMYDVIQSY
     NKMDCGSLMY AYGITPAVDP MFECKPAYDI CHMIANQLGI GSKFTNGGMT YLDQVRKVFA
     EFKKSNPWIQ GDTFEEFVSF GPQRRPAGEH PNVGKIRDFI TDPIASPLGT PSGKVEIYSQ
     YFEGKQTQAE GTDEINPLPV YFACDESYED ATASEFPLQC INYHGKHSAH SIHASTPWLN
     EVLEHHLWLN PIDAGAAGVI NGQKVIVESR RGKLEITARV TPRIVPGVVA MPQGQWRRMK
     GDIDVGGCAN TLTDSKPSPV AKSFRSNTNR VRVYSA
//

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