(data stored in SCRATCH zone)

SWISSPROT: A8FPR9_SHESH

ID   A8FPR9_SHESH            Unreviewed;       838 AA.
AC   A8FPR9;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 75.
DE   SubName: Full=Anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family {ECO:0000313|EMBL:ABV34842.1};
GN   OrderedLocusNames=Ssed_0229 {ECO:0000313|EMBL:ABV34842.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34842.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34842.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34842.1,
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:SAAS00648863}.
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DR   EMBL; CP000821; ABV34842.1; -; Genomic_DNA.
DR   RefSeq; WP_012004368.1; NC_009831.1.
DR   ProteinModelPortal; A8FPR9; -.
DR   STRING; 425104.Ssed_0229; -.
DR   EnsemblBacteria; ABV34842; ABV34842; Ssed_0229.
DR   KEGG; sse:Ssed_0229; -.
DR   eggNOG; ENOG4107QY8; Bacteria.
DR   eggNOG; COG0243; LUCA.
DR   HOGENOM; HOG000284390; -.
DR   KO; K07306; -.
DR   OMA; ANGEQSM; -.
DR   OrthoDB; POG091H05B3; -.
DR   BioCyc; SSED425104:GH7Q-232-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; IPR027467; MopterinOxRdtase_cofactor_BS.
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   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; PS00551; MOLYBDOPTERIN_PROK_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FPR9.
DR   SWISS-2DPAGE; A8FPR9.
KW   4Fe-4S {ECO:0000256|SAAS:SAAS00495824};
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       41    102       4Fe-4S Mo/W bis-MGD-type.
FT                                {ECO:0000259|PROSITE:PS51669}.
SQ   SEQUENCE   838 AA;  91049 MW;  EBFE211585255380 CRC64;
     MERRSFLKMS AAMGCAASVT GCKTSSDDAN VVPPQPPVGE EQITWSSCLV NCGSNCPVKV
     FSRDGVITRV ETDHDVADGD DVYQVRACAR GRSLRQRTYA VDRLKTPMKR VGKRGEGKFV
     PISWDEAAKT IGTKLTSVIA EHGNKAIFRS YGSGAYYGFA SNACFNRLFN LNGGCLNAYG
     NYSWAQQMEA AKHTFGTGST SGSSTVTLAN SDFLLGVAYN PSEIRQSGSG EGYDYLKALQ
     KSNGLKVVMI DPRYTDSMLG KESKWLPIRP GTDAAFAEAI AYQMISSGWV DQNSLSFINK
     YAVGFDAASI TAQKELFANS GDATKQEYAK VMKPEENYRD YILSQGVYAD QPLKTSEWAE
     KITGIPAAQL EQIATDLQNA KAPYIVVGAG VNRQANGEQS MRALYMLSVL TGKLGTLGAS
     NGELPSMSGM YRAGIPTGSN PVKESISFFT WSEAIHNGET MTARSHGVRG TDGLDTPLGT
     NIKVIISASD SSLLNQHAEI NNTAKILEDE TGVELIVSCD CWMTPGAKFA DIILPDTSWL
     ESNDLVNDSY ASGALGYITA MKSAIEPMWD CKSMYEASAL IAKYMGCEAE FTEGKTEEQW
     LEELYQKTKD SSTNLGVVPA FPATYKEAQE IGFFRKNMND NHVALKSYIN GGKALSTPSG
     KIEIYSAELA WRAANWDQEL TTDVKGDTIT AIPQYTVTWD GYEDEDTSTD YPIQLAGYHT
     KGRTHSSYHN VPWLREAVED AVWVNPMDAA ENGLSAGDKI EMYNERGSIA VKVRITPRVA
     PGVFALGQGA WFKPGNTVGS TGHIIDEGGA INTLTRYQPS PVAKGNPQHT NRVAIKKI
//

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