SIR_SYNY3
ID SIR_SYNY3 Reviewed; 635 AA.
AC P72854;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Sulfite reductase [ferredoxin];
DE EC=1.8.7.1;
GN Name=sir; OrderedLocusNames=slr0963;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: Catalyzes the reduction of sulfite to sulfide, a step in the
CC biosynthesis of sulfur-containing amino acids and cofactors.
CC {ECO:0000250|UniProtKB:P9WJ03}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 H2O + hydrogen sulfide + 6 oxidized [2Fe-2S]-[ferredoxin] =
CC 7 H(+) + 6 reduced [2Fe-2S]-[ferredoxin] + sulfite;
CC Xref=Rhea:RHEA:23132, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359,
CC ChEBI:CHEBI:29919, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.8.7.1;
CC Evidence={ECO:0000250|UniProtKB:P9WJ03};
CC -!- COFACTOR:
CC Name=siroheme; Xref=ChEBI:CHEBI:60052; Evidence={ECO:0000250};
CC Note=Binds 1 siroheme per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- INTERACTION:
CC P72854; P52231: trxA; NbExp=3; IntAct=EBI-862835, EBI-862916;
CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC family. {ECO:0000305}.
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DR EMBL; BA000022; BAA16869.1; -; Genomic_DNA.
DR PIR; S74718; S74718.
DR AlphaFoldDB; P72854; -.
DR SMR; P72854; -.
DR IntAct; P72854; 4.
DR STRING; 1148.1651943; -.
DR PaxDb; P72854; -.
DR EnsemblBacteria; BAA16869; BAA16869; BAA16869.
DR KEGG; syn:slr0963; -.
DR eggNOG; COG0155; Bacteria.
DR InParanoid; P72854; -.
DR OMA; WQMMLRL; -.
DR PhylomeDB; P72854; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0009337; C:sulfite reductase complex (NADPH); IBA:GO_Central.
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:0050311; F:sulfite reductase (ferredoxin) activity; IBA:GO_Central.
DR GO; GO:0016002; F:sulfite reductase activity; IBA:GO_Central.
DR GO; GO:0000103; P:sulfate assimilation; IBA:GO_Central.
DR Gene3D; 3.30.413.10; -; 2.
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 InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR InterPro; IPR011787; SiR_ferredoxin-dep.
DR PANTHER; PTHR11493; PTHR11493; 1.
DR Pfam; PF01077; NIR_SIR; 2.
DR Pfam; PF03460; NIR_SIR_ferr; 2.
DR PRINTS; PR00397; SIROHAEM.
DR SUPFAM; SSF55124; SSF55124; 2.
DR SUPFAM; SSF56014; SSF56014; 2.
DR TIGRFAMs; TIGR02042; sir; 1.
DR PROSITE; PS00365; NIR_SIR; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Heme; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW Reference proteome; Thioether bond.
FT CHAIN 1..635
FT /note="Sulfite reductase [ferredoxin]"
FT /id="PRO_0000199954"
FT BINDING 451
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 457
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 496
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 500
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 500
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 CROSSLNK 54..139
FT /note="3'-(S-cysteinyl)-tyrosine (Tyr-Cys)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 635 AA; 71441 MW; 91F4A1B139AD7B34 CRC64;
MVTTPTAAPR KPSKVEGIKE RSNYLREPLA TELLNDANYF TDDAVQILKF HGSYQQDNRD
NRVKGQEKDY QFMLRTRNPG GLIPAQLYTA LDDLSKTHGN QTLRVTTRQG LQIHGIVKKD
LKMAIATVVN NLGSTLGACG DINRNVMAPA APFRDKPEYG YAWDYANKVA DLLSPQSGAY
YEIWLDGEKV ISGEEAPEVK AARQKDLNGT NLNDPKEPIY GQQFMPRKFK ISVTVPGDNS
IDVYTHDISL VVITDRHGEL RGFNVLAGGG LGRTHNKEET FARAADPIGY VSKDDVYDLV
KAIVATQRDY GDRHNRRHAR MKYLLADWGV EKFRKQVETY MGKPFQSFKP LPAWRYQDYL
GWHEQGDGKL FFGLSVENGR IKDEGDFQLK TALRKVVDQF QLPLRLTANH NILLYDINAQ
DKAAIEQIFQ QHGVVTDPEA IDTLVRYSMA CPALPTCGLA VTESERIMPS VNARLRDLLN
SLDLPNESIV TRMTGCPNGC ARPYMAEIGF VGSAPNSYQV WLGGSPNQER LAAAYTEKMP
LEQLESLFEP LFVYFKQSRK GKESFGDFCH RVGFTALREF SHGYTAPAKG GKNRKNQRRV
SLSDEMYAQL KARSERDNCP MNQIVQQALT AYLGK
