(data stored in SCRATCH zone)

SWISSPROT: C8W1Y8_DESAS

ID   C8W1Y8_DESAS            Unreviewed;       472 AA.
AC   C8W1Y8;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 51.
DE   SubName: Full=Sulfite reductase, dissimilatory-type alpha subunit {ECO:0000313|EMBL:ACV61042.1};
DE            EC=1.8.99.3 {ECO:0000313|EMBL:ACV61042.1};
GN   OrderedLocusNames=Dtox_0079 {ECO:0000313|EMBL:ACV61042.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61042.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61042.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
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DR   EMBL; CP001720; ACV61042.1; -; Genomic_DNA.
DR   RefSeq; WP_012813494.1; NC_013216.1.
DR   STRING; 485916.Dtox_0079; -.
DR   EnsemblBacteria; ACV61042; ACV61042; Dtox_0079.
DR   KEGG; dae:Dtox_0079; -.
DR   eggNOG; COG2221; LUCA.
DR   HOGENOM; HOG000007658; -.
DR   KO; K11180; -.
DR   OMA; MHCINVM; -.
DR   OrthoDB; 1128731at2; -.
DR   BioCyc; DACE485916:G1GFV-83-MONOMER; -.
DR   Proteomes; UP000002217; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0018551; F:hydrogensulfite reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR011806; DsrA.
DR   InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR   InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
DR   InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR   Pfam; PF01077; NIR_SIR; 1.
DR   Pfam; PF03460; NIR_SIR_ferr; 1.
DR   SUPFAM; SSF55124; SSF55124; 1.
DR   TIGRFAMs; TIGR02064; dsrA; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   4: Predicted;
DR   PRODOM; C8W1Y8.
DR   SWISS-2DPAGE; C8W1Y8.
KW   4Fe-4S {ECO:0000256|SAAS:SAAS00296119};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Iron {ECO:0000256|SAAS:SAAS00296139};
KW   Iron-sulfur {ECO:0000256|SAAS:SAAS00296144};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00296121};
KW   Oxidoreductase {ECO:0000313|EMBL:ACV61042.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217}.
FT   DOMAIN      329    357       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
SQ   SEQUENCE   472 AA;  53709 MW;  8FA430A5D4FE6966 CRC64;
     MSFEPQEPKK VIKYEDVRIY TDAEINNYTE EELKAFKIKY DIPDLEELEN GPWPSFVADA
     KQAALHRSKL PADRMLIDPN GVEDMLGQLQ VSFDEGETHW KHGGIVGVFG YGGGVIGRYS
     DLPERFPSIA HFHTVRLNQP ASKFYNTDFL KSLCDLWDYR GSGMLNLHGS TGDIILLGTT
     TEQLEPIFFE VTHVMDQDIG GSGSNLRTPS CCIGKARCEW ALYDTQEMCY EMTNYYQDEL
     HRPAFPYKFK FKFDGCPNGC VASIARSDMS FIGTWRDDIR IDQAAVQAYI NGEYAPNAGA
     HAGKDWGKFD IKKEVLDLCP TKCMWMEGGE LKIDNAECTR CMHCIAVMPR ALRPGTDTGV
     TILCGAKAPI LDGAQMSTLI VPFMKAEPPY DNIKEFIEKV WELWMEEGRN RERLGEMIQR
     ITLPKFIETI GLPATPQMVK APRSNPYIFW KEEDVPGGWD RDINEYRARH KR
//

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