DSRB_ARCFU
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 03-AUG-2022, entry version 132.
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 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 332-359, FUNCTION,
RP AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
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: physico-
RT chemical properties of the enzyme and cloning, sequencing and analysis of
RT the reductase genes.";
RL J. Gen. Microbiol. 139:1817-1828(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) IN COMPLEX WITH DSRB; IRON-SULFUR
RP (4FE-4S) AND SIROHEME, SUBUNIT, COFACTOR, AND REACTION MECHANISM.
RX PubMed=18495156; DOI=10.1016/j.jmb.2008.04.027;
RA Schiffer A., Parey K., Warkentin E., Diederichs K., Huber H., Stetter K.O.,
RA 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; IRON-SULFUR
RP (4FE-4S); SIROHEME AND HYDROGENSULFITE, COFACTOR, SUBUNIT, CATALYTIC
RP 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 Archaeoglobus
RT fulgidus.";
RL Biochemistry 49:8912-8921(2010).
CC -!- FUNCTION: Catalyzes the reduction of sulfite to sulfide. This is the
CC 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-COMP:11723,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:17499, ChEBI:CHEBI:29919,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:50058; EC=1.8.99.5;
CC Evidence={ECO:0000269|PubMed:20822098, ECO:0000269|PubMed:7691984};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[DsrC protein]-S-sulfanyl-L-cysteine/L-cysteine + 3 A + 3 H2O
CC = [DsrC protein]-disulfide + 3 AH2 + 2 H(+) + sulfite;
CC Xref=Rhea:RHEA:47020, Rhea:RHEA-COMP:11722, Rhea:RHEA-COMP:11724,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:50058, ChEBI:CHEBI:61963; EC=1.8.99.5;
CC Evidence={ECO:0000269|PubMed:20822098, ECO:0000269|PubMed:7691984};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:18495156, 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, 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 degrees
CC 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 is
CC found in the soluble fraction it may be membrane-associated in vivo.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB90811.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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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 AlphaFoldDB; 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 HOGENOM; CLU_044442_0_0_2; -.
DR OMA; INTCTAF; -.
DR OrthoDB; 58856at2157; -.
DR PhylomeDB; Q59110; -.
DR BioCyc; MetaCyc:MON-12501; -.
DR BRENDA; 1.8.99.5; 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 Gene3D; 3.30.413.10; -; 1.
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 InterPro; IPR045169; NO2/SO3_Rdtase_4Fe4S_prot.
DR InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR PANTHER; PTHR11493; PTHR11493; 1.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF01077; NIR_SIR; 1.
DR Pfam; PF03460; NIR_SIR_ferr; 1.
DR SUPFAM; SSF55124; SSF55124; 1.
DR SUPFAM; SSF56014; SSF56014; 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; Direct protein sequencing; Heme; Iron; Iron-sulfur;
KW Membrane; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..366
FT /note="Sulfite reductase, dissimilatory-type subunit beta"
FT /id="PRO_0000080027"
FT DOMAIN 232..262
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 140
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18495156,
FT ECO:0000269|PubMed:20822098, ECO:0007744|PDB:3MM5,
FT ECO:0007744|PDB:3MMC"
FT BINDING 177
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18495156,
FT ECO:0000269|PubMed:20822098, ECO:0007744|PDB:3MM5,
FT ECO:0007744|PDB:3MMC"
FT BINDING 178
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18495156,
FT ECO:0000269|PubMed:20822098, ECO:0007744|PDB:3MM5,
FT ECO:0007744|PDB:3MMC"
FT BINDING 182
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18495156,
FT ECO:0000269|PubMed:20822098, ECO:0007744|PDB:3MM5,
FT ECO:0007744|PDB:3MMC"
FT BINDING 182
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:0000305|PubMed:18495156,
FT ECO:0000305|PubMed:20822098"
FT BINDING 220
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18495156,
FT ECO:0000269|PubMed:20822098, ECO:0007744|PDB:3MM5,
FT ECO:0007744|PDB:3MMC"
FT BINDING 241
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18495156,
FT ECO:0000269|PubMed:20822098, ECO:0007744|PDB:3MM5,
FT ECO:0007744|PDB:3MMC"
FT BINDING 244
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18495156,
FT ECO:0000269|PubMed:20822098, ECO:0007744|PDB:3MM5,
FT ECO:0007744|PDB:3MMC"
FT BINDING 247
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18495156,
FT ECO:0000269|PubMed:20822098, ECO:0007744|PDB:3MM5,
FT ECO:0007744|PDB:3MMC"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 21..26
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 64..77
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:3MM5"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 159..163
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 188..195
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 204..210
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 213..218
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:3MM5"
FT TURN 229..232
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 246..250
FT /evidence="ECO:0007829|PDB:3MM5"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:3MM7"
FT STRAND 283..290
FT /evidence="ECO:0007829|PDB:3MM5"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 297..313
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 320..327
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 329..336
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:3MM7"
FT HELIX 353..357
FT /evidence="ECO:0007829|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
