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Database: UniProt
Entry: Q58280
LinkDB: Q58280
Original site: Q58280 
ID   FSR_METJA               Reviewed;         620 AA.
AC   Q58280;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JAN-2019, entry version 112.
DE   RecName: Full=Coenzyme F420-dependent sulfite reductase {ECO:0000303|PubMed:16048999};
DE            EC=1.8.98.3 {ECO:0000269|PubMed:16048999};
DE   AltName: Full=Sulfite reductase (coenzyme F420) {ECO:0000305};
GN   Name=fsr {ECO:0000303|PubMed:16048999}; OrderedLocusNames=MJ0870;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 /
OS   JCM 10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci;
OC   Methanococcales; Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D.,
RA   Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D.,
RA   Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I.,
RA   Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A.,
RA   Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D.,
RA   Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C.,
RA   Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M.,
RA   Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP   INDUCTION, DOMAIN, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16048999; DOI=10.1074/jbc.M503492200;
RA   Johnson E.F., Mukhopadhyay B.;
RT   "A new type of sulfite reductase, a novel coenzyme F420-dependent
RT   enzyme, from the methanarchaeon Methanocaldococcus jannaschii.";
RL   J. Biol. Chem. 280:38776-38786(2005).
RN   [3]
RP   FUNCTION, AND EXPRESSION IN M.MARIPALUDIS.
RX   PubMed=18378657; DOI=10.1128/AEM.00098-08;
RA   Johnson E.F., Mukhopadhyay B.;
RT   "Coenzyme F420-dependent sulfite reductase-enabled sulfite
RT   detoxification and use of sulfite as a sole sulfur source by
RT   Methanococcus maripaludis.";
RL   Appl. Environ. Microbiol. 74:3591-3595(2008).
CC   -!- FUNCTION: Catalyzes the reduction of sulfite to sulfide using
CC       reduced F420 as the electron source. Involved in sulfite
CC       detoxification and assimilation. Cannot use NADH or NADPH.
CC       {ECO:0000269|PubMed:16048999, ECO:0000269|PubMed:18378657}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + 3 H2O + hydrogen sulfide + 3 oxidized coenzyme
CC         F420-(gamma-Glu)(n) = 3 reduced coenzyme F420-(gamma-Glu)(n) +
CC         sulfite; Xref=Rhea:RHEA:42808, Rhea:RHEA-COMP:12939, Rhea:RHEA-
CC         COMP:14378, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:133980,
CC         ChEBI:CHEBI:139511; EC=1.8.98.3;
CC         Evidence={ECO:0000269|PubMed:16048999};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00711};
CC       Note=Binds 4 [4Fe-4S] cluster. {ECO:0000255|PROSITE-
CC       ProRule:PRU00711};
CC   -!- COFACTOR:
CC       Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC         Evidence={ECO:0000250|UniProtKB:Q59109};
CC       Note=Binds 1 siroheme per subunit. {ECO:0000250|UniProtKB:Q59109};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=12.2 uM for sulfite {ECO:0000269|PubMed:16048999};
CC         KM=21.2 uM for reduced coenzyme F420
CC         {ECO:0000269|PubMed:16048999};
CC       pH dependence:
CC         Optimum pH is 7.0. {ECO:0000269|PubMed:16048999};
CC       Temperature dependence:
CC         Optimum temperature is above 95 degrees Celsius.
CC         {ECO:0000269|PubMed:16048999};
CC   -!- INDUCTION: Induced by sulfite. {ECO:0000269|PubMed:16048999}.
CC   -!- DOMAIN: Contains an N-terminal H(2)F420 dehydrogenase domain and a
CC       C-terminal dissimilatory-type siroheme sulfite reductase domain.
CC       {ECO:0000269|PubMed:16048999}.
CC   -!- MISCELLANEOUS: Expression in Methanococcus maripaludis, a sulfite-
CC       sensitive methanogen, leads to sulfite detoxification and use of
CC       sulfite as a sole sulfur source by M. maripaludis.
CC       {ECO:0000269|PubMed:18378657}.
CC   -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S
CC       domain family. {ECO:0000305}.
DR   EMBL; L77117; AAB98876.1; -; Genomic_DNA.
DR   PIR; F64408; F64408.
DR   RefSeq; WP_010870385.1; NC_000909.1.
DR   ProteinModelPortal; Q58280; -.
DR   SMR; Q58280; -.
DR   STRING; 243232.MJ_0870; -.
DR   PRIDE; Q58280; -.
DR   EnsemblBacteria; AAB98876; AAB98876; MJ_0870.
DR   GeneID; 1451759; -.
DR   KEGG; mja:MJ_0870; -.
DR   eggNOG; arCOG02650; Archaea.
DR   eggNOG; COG1035; LUCA.
DR   eggNOG; COG2221; LUCA.
DR   InParanoid; Q58280; -.
DR   KO; K21816; -.
DR   OMA; YFPYLAK; -.
DR   OrthoDB; 49654at2157; -.
DR   BioCyc; MJAN243232:G1GKE-945-MONOMER; -.
DR   BRENDA; 1.8.98.3; 3260.
DR   Proteomes; UP000000805; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR007516; Co_F420_Hydgase/DH_bsu_N.
DR   InterPro; IPR007525; FrhB_FdhB_C.
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   InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR   Pfam; PF00037; Fer4; 2.
DR   Pfam; PF04432; FrhB_FdhB_C; 1.
DR   Pfam; PF04422; FrhB_FdhB_N; 1.
DR   Pfam; PF01077; NIR_SIR; 1.
DR   Pfam; PF03460; NIR_SIR_ferr; 1.
DR   PRINTS; PR00397; SIROHAEM.
DR   SUPFAM; SSF55124; SSF55124; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 3.
DR   PROSITE; PS00365; NIR_SIR; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Complete proteome; Heme; Iron; Iron-sulfur; Metal-binding;
KW   Oxidoreductase; Reference proteome; Repeat.
FT   CHAIN         1    620       Coenzyme F420-dependent sulfite
FT                                reductase.
FT                                /FTId=PRO_0000199970.
FT   DOMAIN        6     35       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      486    515       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      520    544       4Fe-4S ferredoxin-type 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        15     15       Iron-sulfur (4Fe-4S) 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        18     18       Iron-sulfur (4Fe-4S) 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        21     21       Iron-sulfur (4Fe-4S) 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        25     25       Iron-sulfur (4Fe-4S) 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       428    428       Iron-sulfur (4Fe-4S) 2.
FT                                {ECO:0000250|UniProtKB:Q59109}.
FT   METAL       434    434       Iron-sulfur (4Fe-4S) 2.
FT                                {ECO:0000250|UniProtKB:Q59109}.
FT   METAL       468    468       Iron-sulfur (4Fe-4S) 2.
FT                                {ECO:0000250|UniProtKB:Q59109}.
FT   METAL       472    472       Iron (siroheme axial ligand).
FT                                {ECO:0000250|UniProtKB:Q59109}.
FT   METAL       472    472       Iron-sulfur (4Fe-4S) 2.
FT                                {ECO:0000250|UniProtKB:Q59109}.
FT   METAL       495    495       Iron-sulfur (4Fe-4S) 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       498    498       Iron-sulfur (4Fe-4S) 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       501    501       Iron-sulfur (4Fe-4S) 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       505    505       Iron-sulfur (4Fe-4S) 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       524    524       Iron-sulfur (4Fe-4S) 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       527    527       Iron-sulfur (4Fe-4S) 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       530    530       Iron-sulfur (4Fe-4S) 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       534    534       Iron-sulfur (4Fe-4S) 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
SQ   SEQUENCE   620 AA;  69794 MW;  9D71D2580D7D0BA8 CRC64;
     MYEWKLNEIV DSGVCARCGT CTIVCPNGIL TFDERPKLID ECLRKGHGMC FEVCPRVSSA
     KYQIKIREKF YEKYYYAKSD IEGQDGGVVT AFLKYLLENG KIDGAIVVGD ECWKPVSLVV
     QNAEDLLKTA KSKYAISTLD ALRKAGEMGL EKVAVVGLPC QINGLRKLQY FPYHAKHDLE
     LGRNGKPVKL PKIEYLIGLF CTEKFRYDNM KEVLSKHGID IEKVEKFDIK KGKLLVYVNG
     EKKEFDLKEF EICSGCKMCR DFDAEMADVS VGCVGSPDGY STIIIRTEKG EEIKNAVELK
     EGVNLEEIEK LRQLKLKRFK KEVERRRENN EYVSFYWTAD YGGIGKRADG TYFIRVRAKP
     GGWYKPEEIK EILDIAEEYN AKIKVTDRAG YELHGISGFD VEDIVLRLRE KGLLTGSEGP
     LVRATLACPG GGNCSSGLVD TTELARIIED NFKERPAPYK FKIAISGCPN GCVRPQVHDI
     GIAGVKYPKV NEEKCNGCGR CAEVCKVEAI DIRGETSYTN YNVCVGCGKC IKNCPNEARE
     VKEEGYLVYV GGKTGREVVE GVKMKLMSVD EIINFIDKVL VVYGKYAEKP QRERLAAVMK
     RVGYGKFLEE VKELMKKEIC
//
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