SIR_DESVH
ID SIR_DESVH Reviewed; 218 AA.
AC Q05805;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Sulfite reductase, assimilatory-type;
DE EC=1.8.-.-;
GN OrderedLocusNames=DVU_1597;
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=882;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1911781; DOI=10.1021/bi00105a013;
RA Tan J., Helms L.R., Swenson R.P., Cowan J.A.;
RT "Primary structure of the assimilatory-type sulfite reductase from
RT Desulfovibrio vulgaris (Hildenborough): cloning and nucleotide sequence of
RT the reductase gene.";
RL Biochemistry 30:9900-9907(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA Wall J.D., Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
CC -!- FUNCTION: This enzyme catalyzes the 6-electron reduction of sulfite to
CC sulfide. This is one of several activities required for the
CC biosynthesis of L-cysteine from sulfate.
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DR EMBL; M77241; AAA23383.1; -; Genomic_DNA.
DR EMBL; AE017285; AAS96075.1; -; Genomic_DNA.
DR PIR; A40347; A40347.
DR RefSeq; WP_010938888.1; NZ_CABHLV010000001.1.
DR RefSeq; YP_010816.1; NC_002937.3.
DR AlphaFoldDB; Q05805; -.
DR SMR; Q05805; -.
DR STRING; 882.DVU_1597; -.
DR PaxDb; Q05805; -.
DR PRIDE; Q05805; -.
DR EnsemblBacteria; AAS96075; AAS96075; DVU_1597.
DR KEGG; dvu:DVU_1597; -.
DR PATRIC; fig|882.5.peg.1472; -.
DR eggNOG; COG1251; Bacteria.
DR HOGENOM; CLU_072599_0_0_7; -.
DR OMA; TTFCKRG; -.
DR PhylomeDB; Q05805; -.
DR Proteomes; UP000002194; 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 GO; GO:0019344; P:cysteine biosynthetic process; 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; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR InterPro; IPR017220; Sulphite_reductase_assimil.
DR Pfam; PF01077; NIR_SIR; 1.
DR Pfam; PF03460; NIR_SIR_ferr; 1.
DR PIRSF; PIRSF037487; Sulfite_red_assimil; 1.
DR PRINTS; PR00397; SIROHAEM.
DR SUPFAM; SSF55124; SSF55124; 1.
DR SUPFAM; SSF56014; SSF56014; 1.
DR PROSITE; PS00365; NIR_SIR; 1.
PE 4: Predicted;
KW 4Fe-4S; Amino-acid biosynthesis; Cysteine biosynthesis; Heme; Iron;
KW Iron-sulfur; Metal-binding; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..218
FT /note="Sulfite reductase, assimilatory-type"
FT /id="PRO_0000199967"
FT BINDING 91
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 135
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"
FT CONFLICT 138
FT /note="S -> T (in Ref. 1; AAA23383)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 218 AA; 23845 MW; EB22CFD6003AC3EB CRC64;
MSDEPKGAIL QRDKLTYAIV PRTPCGLLTP DVLDAVSRVC RKYEVPIIKI TSGQRLALVG
MKKEAVEPMW EELRLDVGRA VELCVHYVQA CPGTAVCRFG LQDSLGIGVA IEEEYVGHDF
PAKVKFGISG CPFCCGESYL RDVGLVGTKK GWTLIVGGNS GGHPRIGDVL AEELSTDEAK
GLIRKFMEFY RDNSGKRLRV SKFVEKTGIE AIRQAVLG
