DSRA_ALLVD
ID DSRA_ALLVD Reviewed; 417 AA.
AC O33998; D3RSN1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Sulfite reductase, dissimilatory-type subunit alpha;
DE EC=1.8.99.5 {ECO:0000250|UniProtKB:Q59109};
DE AltName: Full=Dissimilatory sulfite reductase subunit alpha;
DE AltName: Full=Hydrogensulfite reductase subunit alpha;
GN Name=dsrA; OrderedLocusNames=Alvin_1251;
OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS 10441 / D) (Chromatium vinosum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Allochromatium.
OX NCBI_TaxID=572477;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9308173; DOI=10.1099/00221287-143-9-2891;
RA Hipp W.M., Pott A.S., Thum-Schmitz N., Faath I., Dahl C., Trueper H.G.;
RT "Towards the phylogeny of APS reductases and sirohaem sulfite reductases in
RT sulfate-reducing and sulfur-oxidizing prokaryotes.";
RL Microbiology 143:2891-2902(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX PubMed=22675582; DOI=10.4056/sigs.2335270;
RA Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL Stand. Genomic Sci. 5:311-330(2011).
CC -!- FUNCTION: Catalyzes the reduction of sulfite to sulfide. This is the
CC terminal oxidation reaction in sulfate respiration.
CC {ECO:0000250|UniProtKB:Q59109}.
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:Q59109};
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:Q59109};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:Q59109};
CC Note=Binds 2 [4Fe-4S] clusters per subunit.
CC {ECO:0000250|UniProtKB:Q59109};
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};
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DR EMBL; U84760; AAC35394.1; -; Genomic_DNA.
DR EMBL; CP001896; ADC62190.1; -; Genomic_DNA.
DR RefSeq; WP_012970464.1; NC_013851.1.
DR AlphaFoldDB; O33998; -.
DR SMR; O33998; -.
DR STRING; 572477.Alvin_1251; -.
DR EnsemblBacteria; ADC62190; ADC62190; Alvin_1251.
DR KEGG; alv:Alvin_1251; -.
DR eggNOG; COG2221; Bacteria.
DR HOGENOM; CLU_660112_0_0_6; -.
DR OMA; MHCLNVM; -.
DR OrthoDB; 1128731at2; -.
DR BioCyc; MetaCyc:MON-12320; -.
DR BRENDA; 1.8.99.5; 257.
DR Proteomes; UP000001441; 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:0018551; F:hydrogensulfite reductase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.413.10; -; 1.
DR InterPro; IPR011806; DsrA.
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.
DR SUPFAM; SSF56014; SSF56014; 1.
DR TIGRFAMs; TIGR02064; dsrA; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Heme; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..417
FT /note="Sulfite reductase, dissimilatory-type subunit alpha"
FT /id="PRO_0000080026"
FT BINDING 170
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q59109"
FT BINDING 176
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q59109"
FT BINDING 214
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q59109"
FT BINDING 218
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q59109"
FT BINDING 218
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 264
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q59109"
FT BINDING 284
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q59109"
FT BINDING 287
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q59109"
FT BINDING 290
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q59109"
SQ SEQUENCE 417 AA; 46791 MW; 474680A622F37B40 CRC64;
MAIDKHATPM LDQLETGPWP SFISGIKRLR DQHPDARINA VTNDLLGQLE HSYETRKGYW
KGGTVSVFGY GGGIIPRFSE VGKVFPSSKE FHTVRVQPPA GNHYTTAMLR QLADTWEKYG
SGLITFHGQT GNIMFIGVDT PNTQNFFDEI NDYGWDLGGA GPCVRTAMSC VGSARCEMSC
TNELKAHRLL VNNFTDDVHR PALPYKFKFK VSGCPNDCQN AIERSDFAVL GTWRDDMKVD
QAEVKHYIAD KGRQYYIDNV ITRCPTKALS LNDDDTLDVN NRDCVRCMHC LNVMPKALHP
GDDKGVTILI GGKRTLKIGD LMGTVVVPFK KLETEEDYES LVELAETIID FWAENGLEHE
RCGEMIERIG LANFLEGIGI EPDPNMLSHP RQSSYIRMDG WDEAAEEWFA RQAEAGR
