DSVB_MEGG1
ID DSVB_MEGG1 Reviewed; 262 AA.
AC P94694;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Sulfite reductase, dissimilatory-type subunit beta;
DE EC=1.8.99.5 {ECO:0000250|UniProtKB:P45575};
DE AltName: Full=Desulfoviridin subunit beta;
DE AltName: Full=Dissimilatory sulfite reductase subunit beta;
DE Short=dSiR beta;
DE AltName: Full=Hydrogensulfite reductase subunit beta;
DE Flags: Fragment;
GN Name=dsrB;
OS Megalodesulfovibrio gigas (strain ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM
OS B-1759) (Desulfovibrio gigas).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Megalodesulfovibrio.
OX NCBI_TaxID=1121448;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM B-1759;
RA Hipp W.M., Trueper H.G.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reduction of sulfite to sulfide. This is the
CC terminal oxidation reaction in sulfate respiration, a process catalyzed
CC by the sulfate-reducing bacteria. {ECO:0000250|UniProtKB:P45575}.
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:0000250|UniProtKB:P45575};
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:0000250|UniProtKB:P45575};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P45575};
CC Note=Binds 2 [4Fe-4S] clusters per subunit.
CC {ECO:0000250|UniProtKB:P45575};
CC -!- COFACTOR:
CC Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC Evidence={ECO:0000250|UniProtKB:P45575};
CC Note=Binds 1 siroheme per subunit. {ECO:0000250|UniProtKB:P45575};
CC -!- SUBUNIT: Heterohexamer of two alpha, two beta and two gamma subunits.
CC {ECO:0000250|UniProtKB:P45575}.
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DR EMBL; U80961; AAB41002.1; -; Genomic_DNA.
DR AlphaFoldDB; P94694; -.
DR SMR; P94694; -.
DR STRING; 1121448.DGI_0689; -.
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 Gene3D; 3.30.413.10; -; 1.
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; PF01077; NIR_SIR; 1.
DR Pfam; PF03460; NIR_SIR_ferr; 1.
DR SUPFAM; SSF55124; SSF55124; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Oxidoreductase.
FT CHAIN 1..>262
FT /note="Sulfite reductase, dissimilatory-type subunit beta"
FT /id="PRO_0000080031"
FT BINDING 151
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P45575"
FT BINDING 188
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P45575"
FT BINDING 189
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P45575"
FT BINDING 193
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P45575"
FT BINDING 193
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:P45575"
FT BINDING 231
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P45575"
FT BINDING 258
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P45575"
FT BINDING 261
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P45575"
FT NON_TER 262
SQ SEQUENCE 262 AA; 28569 MW; 2D4DA1C19B7DCE5D CRC64;
MAFISSGYNP AKPMENRITD IGPRKFTEFF PPVIAKNAGN WDYHEILEPG ILVHVAKNGD
KVFTVRCGAA RLMSTSHIRE ACEIAKKFCN GHLRFTTRNN IEFMVDNEET LKALVADLKT
RKFAAGSFKF PIGGTGASIS NIVHTQGWVY CHTPATDASG PVKAVMDELF EEFTSMRLPA
IVRVSLACCI NMCGAVHCSD IGLVGIHRKP PMIDHENLAN LCEIPLAVAA CPTAAVKPIT
AEVNGQKVKS VAINNDRCMY CG
