FSR_METJA
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 03-AUG-2022, entry version 122.
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 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC 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., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA 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, INDUCTION,
RP 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 enzyme,
RT 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 detoxification
RT and use of sulfite as a sole sulfur source by Methanococcus maripaludis.";
RL Appl. Environ. Microbiol. 74:3591-3595(2008).
CC -!- FUNCTION: Catalyzes the reduction of sulfite to sulfide using reduced
CC F420 as the electron source. Involved in sulfite detoxification and
CC assimilation. Cannot use NADH or NADPH. {ECO:0000269|PubMed:16048999,
CC ECO:0000269|PubMed:18378657}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + 3 H2O + hydrogen sulfide + 3 oxidized coenzyme F420-
CC (gamma-L-Glu)(n) = 3 reduced coenzyme F420-(gamma-L-Glu)(n) +
CC sulfite; Xref=Rhea:RHEA:42808, Rhea:RHEA-COMP:12939, Rhea:RHEA-
CC COMP:14378, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359,
CC ChEBI:CHEBI:29919, ChEBI:CHEBI:133980, ChEBI:CHEBI:139511;
CC EC=1.8.98.3; 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-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 {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 C-
CC 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 domain
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L77117; AAB98876.1; -; Genomic_DNA.
DR PIR; F64408; F64408.
DR RefSeq; WP_010870385.1; NC_000909.1.
DR PDB; 7NP8; X-ray; 2.30 A; A/B/C/D=1-620.
DR PDBsum; 7NP8; -.
DR AlphaFoldDB; 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; arCOG02061; Archaea.
DR HOGENOM; CLU_428041_0_0_2; -.
DR InParanoid; Q58280; -.
DR OMA; GDECWKP; -.
DR OrthoDB; 49654at2157; -.
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:0052592; F:oxidoreductase activity, acting on CH or CH2 groups, with an iron-sulfur protein as acceptor; IBA:GO_Central.
DR Gene3D; 3.30.413.10; -; 1.
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; IPR045220; FRHB/FDHB/HCAR-like.
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; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR PANTHER; PTHR31332; PTHR31332; 1.
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 SUPFAM; SSF56014; SSF56014; 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 3D-structure; 4Fe-4S; Heme; Iron; Iron-sulfur; Metal-binding;
KW Oxidoreductase; Reference proteome; Repeat.
FT CHAIN 1..620
FT /note="Coenzyme F420-dependent sulfite reductase"
FT /id="PRO_0000199970"
FT DOMAIN 6..35
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 486..515
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 520..544
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 15
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 18
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 21
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 25
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 428
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q59109"
FT BINDING 434
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q59109"
FT BINDING 468
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q59109"
FT BINDING 472
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q59109"
FT BINDING 472
FT /ligand="siroheme"
FT /ligand_id="ChEBI:CHEBI:60052"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q59109"
FT BINDING 495
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 498
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 501
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 505
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 524
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 527
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 530
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 534
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="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
