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Database: UniProt
Entry: Q59110
LinkDB: Q59110
Original site: Q59110 
ID   DSRB_ARCFU              Reviewed;         366 AA.
AC   Q59110;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   10-APR-2019, entry version 120.
DE   RecName: Full=Sulfite reductase, dissimilatory-type subunit beta;
DE            EC=1.8.99.5 {ECO:0000269|PubMed:20822098, ECO:0000269|PubMed:7691984};
DE   AltName: Full=Hydrogensulfite reductase subunit beta;
GN   Name=dsrB; OrderedLocusNames=AF_0424;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM
OS   9628 / NBRC 100126).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales;
OC   Archaeoglobaceae; Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 332-359,
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
RX   PubMed=7691984; DOI=10.1099/00221287-139-8-1817;
RA   Dahl C., Kredich N.M., Deutzmann R., Trueper H.G.;
RT   "Dissimilatory sulphite reductase from Archaeoglobus fulgidus:
RT   physico-chemical properties of the enzyme and cloning, sequencing and
RT   analysis of the reductase genes.";
RL   J. Gen. Microbiol. 139:1817-1828(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E.,
RA   Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D.,
RA   Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C.,
RA   Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G., Gill S.R.,
RA   Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J.,
RA   Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A.,
RA   Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A.,
RA   Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P.,
RA   Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C.,
RA   Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O.,
RA   Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-
RT   reducing archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) IN COMPLEX WITH DSRB;
RP   IRON-SULFUR (4FE-4S) AND SIROHEME, SUBUNIT, COFACTOR, AND REACTION
RP   MECHANISM.
RX   PubMed=18495156; DOI=10.1016/j.jmb.2008.04.027;
RA   Schiffer A., Parey K., Warkentin E., Diederichs K., Huber H.,
RA   Stetter K.O., Kroneck P.M.H., Ermler U.;
RT   "Structure of the dissimilatory sulfite reductase from the
RT   hyperthermophilic archaeon Archaeoglobus fulgidus.";
RL   J. Mol. Biol. 379:1063-1074(2008).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH DSRB;
RP   IRON-SULFUR (4FE-4S); SIROHEME AND HYDROGENSULFITE, COFACTOR, SUBUNIT,
RP   CATALYTIC ACTIVITY, AND REACTION MECHANISM.
RX   PubMed=20822098; DOI=10.1021/bi100781f;
RA   Parey K., Warkentin E., Kroneck P.M., Ermler U.;
RT   "Reaction cycle of the dissimilatory sulfite reductase from
RT   Archaeoglobus fulgidus.";
RL   Biochemistry 49:8912-8921(2010).
CC   -!- FUNCTION: Catalyzes the reduction of sulfite to sulfide. This is
CC       the terminal oxidation reaction in sulfate respiration.
CC       {ECO:0000269|PubMed:7691984}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[DsrC protein]-disulfide + 2 A + 3 H2O + hydrogen sulfide
CC         = [DsrC protein]-dithiol + 2 AH2 + H(+) + sulfite;
CC         Xref=Rhea:RHEA:47008, Rhea:RHEA-COMP:11722, Rhea:RHEA-
CC         COMP:11723, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:29919, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058;
CC         EC=1.8.99.5; Evidence={ECO:0000269|PubMed:20822098,
CC         ECO:0000269|PubMed:7691984};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[DsrC protein]-S-sulfanyl-L-cysteine/L-cysteine + 3 A + 3
CC         H2O = [DsrC protein]-disulfide + 3 AH2 + 2 H(+) + sulfite;
CC         Xref=Rhea:RHEA:47020, Rhea:RHEA-COMP:11722, Rhea:RHEA-
CC         COMP:11724, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:61963;
CC         EC=1.8.99.5; Evidence={ECO:0000269|PubMed:20822098,
CC         ECO:0000269|PubMed:7691984};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000269|PubMed:18495156,
CC         ECO:0000269|PubMed:20822098};
CC       Note=Binds 2 [4Fe-4S] cluster per subunit.
CC       {ECO:0000269|PubMed:18495156, ECO:0000269|PubMed:20822098};
CC   -!- COFACTOR:
CC       Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC         Evidence={ECO:0000269|PubMed:18495156,
CC         ECO:0000269|PubMed:20822098};
CC       Note=Binds 1 siroheme per subunit. {ECO:0000269|PubMed:18495156,
CC       ECO:0000269|PubMed:20822098};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Highly thermostable. Inactive towards methylviologen below 55
CC         degrees Celsius.;
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC       {ECO:0000269|PubMed:18495156, ECO:0000269|PubMed:20822098}.
CC   -!- SUBCELLULAR LOCATION: Membrane. Note=Although the protein complex
CC       is found in the soluble fraction it may be membrane-associated in
CC       vivo.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB90811.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
DR   EMBL; M95624; AAB17214.1; -; Genomic_DNA.
DR   EMBL; AE000782; AAB90811.1; ALT_INIT; Genomic_DNA.
DR   PIR; H69302; H69302.
DR   RefSeq; WP_048064231.1; NC_000917.1.
DR   PDB; 3MM5; X-ray; 1.80 A; B/E=1-366.
DR   PDB; 3MM6; X-ray; 1.90 A; B/E=1-366.
DR   PDB; 3MM7; X-ray; 1.90 A; B/E=1-366.
DR   PDB; 3MM8; X-ray; 2.28 A; B/E=1-366.
DR   PDB; 3MM9; X-ray; 2.10 A; B/E=1-366.
DR   PDB; 3MMA; X-ray; 2.30 A; B/E=1-366.
DR   PDB; 3MMB; X-ray; 2.30 A; B/E=1-366.
DR   PDB; 3MMC; X-ray; 2.04 A; B/E=1-366.
DR   PDBsum; 3MM5; -.
DR   PDBsum; 3MM6; -.
DR   PDBsum; 3MM7; -.
DR   PDBsum; 3MM8; -.
DR   PDBsum; 3MM9; -.
DR   PDBsum; 3MMA; -.
DR   PDBsum; 3MMB; -.
DR   PDBsum; 3MMC; -.
DR   ProteinModelPortal; Q59110; -.
DR   SMR; Q59110; -.
DR   STRING; 224325.AF_0424; -.
DR   EnsemblBacteria; AAB90811; AAB90811; AF_0424.
DR   GeneID; 24793962; -.
DR   KEGG; afu:AF_0424; -.
DR   eggNOG; arCOG02059; Archaea.
DR   eggNOG; COG2221; LUCA.
DR   KO; K11181; -.
DR   OMA; INTCTAF; -.
DR   OrthoDB; 58856at2157; -.
DR   BioCyc; MetaCyc:MONOMER-12501; -.
DR   BRENDA; 1.8.99.3; 414.
DR   EvolutionaryTrace; Q59110; -.
DR   Proteomes; UP000002199; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0018551; F:hydrogensulfite reductase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006790; P:sulfur compound metabolic process; IEA:InterPro.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR011808; DsrB.
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; PF00037; Fer4; 1.
DR   Pfam; PF01077; NIR_SIR; 1.
DR   Pfam; PF03460; NIR_SIR_ferr; 1.
DR   SUPFAM; SSF55124; SSF55124; 1.
DR   TIGRFAMs; TIGR02066; dsrB; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; 4Fe-4S; Complete proteome; Direct protein sequencing;
KW   Heme; Iron; Iron-sulfur; Membrane; Metal-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN         1    366       Sulfite reductase, dissimilatory-type
FT                                subunit beta.
FT                                /FTId=PRO_0000080027.
FT   DOMAIN      232    262       4Fe-4S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       140    140       Iron-sulfur (4Fe-4S) 1.
FT                                {ECO:0000244|PDB:3MM5,
FT                                ECO:0000244|PDB:3MMC,
FT                                ECO:0000269|PubMed:18495156,
FT                                ECO:0000269|PubMed:20822098}.
FT   METAL       177    177       Iron-sulfur (4Fe-4S) 1.
FT                                {ECO:0000244|PDB:3MM5,
FT                                ECO:0000244|PDB:3MMC,
FT                                ECO:0000269|PubMed:18495156,
FT                                ECO:0000269|PubMed:20822098}.
FT   METAL       178    178       Iron-sulfur (4Fe-4S) 1.
FT                                {ECO:0000244|PDB:3MM5,
FT                                ECO:0000244|PDB:3MMC,
FT                                ECO:0000269|PubMed:18495156,
FT                                ECO:0000269|PubMed:20822098}.
FT   METAL       182    182       Iron (siroheme axial ligand).
FT                                {ECO:0000305|PubMed:18495156,
FT                                ECO:0000305|PubMed:20822098}.
FT   METAL       182    182       Iron-sulfur (4Fe-4S) 1.
FT                                {ECO:0000244|PDB:3MM5,
FT                                ECO:0000244|PDB:3MMC,
FT                                ECO:0000269|PubMed:18495156,
FT                                ECO:0000269|PubMed:20822098}.
FT   METAL       220    220       Iron-sulfur (4Fe-4S) 2.
FT                                {ECO:0000244|PDB:3MM5,
FT                                ECO:0000244|PDB:3MMC,
FT                                ECO:0000269|PubMed:18495156,
FT                                ECO:0000269|PubMed:20822098}.
FT   METAL       241    241       Iron-sulfur (4Fe-4S) 2.
FT                                {ECO:0000244|PDB:3MM5,
FT                                ECO:0000244|PDB:3MMC,
FT                                ECO:0000269|PubMed:18495156,
FT                                ECO:0000269|PubMed:20822098}.
FT   METAL       244    244       Iron-sulfur (4Fe-4S) 2.
FT                                {ECO:0000244|PDB:3MM5,
FT                                ECO:0000244|PDB:3MMC,
FT                                ECO:0000269|PubMed:18495156,
FT                                ECO:0000269|PubMed:20822098}.
FT   METAL       247    247       Iron-sulfur (4Fe-4S) 2.
FT                                {ECO:0000244|PDB:3MM5,
FT                                ECO:0000244|PDB:3MMC,
FT                                ECO:0000269|PubMed:18495156,
FT                                ECO:0000269|PubMed:20822098}.
FT   HELIX        15     18       {ECO:0000244|PDB:3MM5}.
FT   HELIX        21     26       {ECO:0000244|PDB:3MM5}.
FT   STRAND       30     37       {ECO:0000244|PDB:3MM5}.
FT   STRAND       40     45       {ECO:0000244|PDB:3MM5}.
FT   STRAND       50     56       {ECO:0000244|PDB:3MM5}.
FT   STRAND       60     63       {ECO:0000244|PDB:3MM5}.
FT   HELIX        64     77       {ECO:0000244|PDB:3MM5}.
FT   STRAND       81     84       {ECO:0000244|PDB:3MM5}.
FT   STRAND       90     95       {ECO:0000244|PDB:3MM5}.
FT   HELIX        97     99       {ECO:0000244|PDB:3MM5}.
FT   HELIX       100    111       {ECO:0000244|PDB:3MM5}.
FT   TURN        121    124       {ECO:0000244|PDB:3MM5}.
FT   HELIX       136    139       {ECO:0000244|PDB:3MM5}.
FT   HELIX       148    157       {ECO:0000244|PDB:3MM5}.
FT   HELIX       159    163       {ECO:0000244|PDB:3MM5}.
FT   STRAND      167    169       {ECO:0000244|PDB:3MM5}.
FT   STRAND      173    178       {ECO:0000244|PDB:3MM5}.
FT   STRAND      182    184       {ECO:0000244|PDB:3MM5}.
FT   HELIX       185    187       {ECO:0000244|PDB:3MM5}.
FT   STRAND      188    195       {ECO:0000244|PDB:3MM5}.
FT   HELIX       204    210       {ECO:0000244|PDB:3MM5}.
FT   HELIX       213    218       {ECO:0000244|PDB:3MM5}.
FT   STRAND      225    228       {ECO:0000244|PDB:3MM5}.
FT   TURN        229    232       {ECO:0000244|PDB:3MM5}.
FT   STRAND      233    236       {ECO:0000244|PDB:3MM5}.
FT   HELIX       238    240       {ECO:0000244|PDB:3MM5}.
FT   HELIX       246    250       {ECO:0000244|PDB:3MM5}.
FT   TURN        259    261       {ECO:0000244|PDB:3MM5}.
FT   STRAND      263    268       {ECO:0000244|PDB:3MM5}.
FT   STRAND      275    277       {ECO:0000244|PDB:3MM7}.
FT   STRAND      283    290       {ECO:0000244|PDB:3MM5}.
FT   TURN        293    295       {ECO:0000244|PDB:3MM5}.
FT   HELIX       297    313       {ECO:0000244|PDB:3MM5}.
FT   HELIX       320    327       {ECO:0000244|PDB:3MM5}.
FT   HELIX       329    336       {ECO:0000244|PDB:3MM5}.
FT   HELIX       342    344       {ECO:0000244|PDB:3MM5}.
FT   STRAND      350    352       {ECO:0000244|PDB:3MM7}.
FT   HELIX       353    357       {ECO:0000244|PDB:3MM5}.
SQ   SEQUENCE   366 AA;  41570 MW;  BA8E4C59216459DA CRC64;
     MVVEGVKTDF GPPYFRDLLH PVIAKNYGKW KYHEVVKPGV IKRVAESGDV IYVVRFGTPR
     LLSIYTVREL CDIADKYSDG YLRWTSRNNV EFFVTDESKI DDLINEVQER VGFPCGGTWD
     AVKGEYGLSN IVHTQGWIHC HTPAIDASGI VKAVMDELYE YFTDHKLPAM CRISLACCAN
     MCGAVHASDI AIVGIHRTPP IPNDEAIRKT CEIPSTVAAC PTGALKPDMK NKTIKVDVEK
     CMYCGNCYTM CPGMPLFDPE NDGAAIMVGG KLSEARRMPE LSKVVVPWVP NEPPRWPTLV
     KYVKQILEAW AANANKHERL IEWVDRIGWE RFFELTGLEF TQHLIDDYRI TPYFYSEFRA
     STQFKW
//
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