SIR_SYNE7
ID SIR_SYNE7 Reviewed; 624 AA.
AC P30008; Q31SB8;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Sulfite reductase [ferredoxin];
DE EC=1.8.7.1;
GN Name=sir; OrderedLocusNames=Synpcc7942_0019;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8347657; DOI=10.1016/0005-2728(93)90037-g;
RA Gisselmann G., Klausmeier P., Schwenn J.D.;
RT "The ferredoxin:sulphite reductase gene from Synechococcus PCC7942.";
RL Biochim. Biophys. Acta 1144:102-106(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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;
CC Note=Binds 1 siroheme per subunit.;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 1 [4Fe-4S] cluster per subunit.;
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC family. {ECO:0000305}.
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DR EMBL; Z11755; CAA77809.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB56051.1; -; Genomic_DNA.
DR RefSeq; WP_011377403.1; NC_007604.1.
DR AlphaFoldDB; P30008; -.
DR SMR; P30008; -.
DR STRING; 1140.Synpcc7942_0019; -.
DR PRIDE; P30008; -.
DR EnsemblBacteria; ABB56051; ABB56051; Synpcc7942_0019.
DR KEGG; syf:Synpcc7942_0019; -.
DR eggNOG; COG0155; Bacteria.
DR HOGENOM; CLU_001975_3_0_3; -.
DR OMA; WQMMLRL; -.
DR OrthoDB; 1588103at2; -.
DR BioCyc; SYNEL:SYNPCC7942_0019-MON; -.
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; IEA:UniProtKB-EC.
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 3: Inferred from homology;
KW 4Fe-4S; Heme; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW Thioether bond.
FT CHAIN 1..624
FT /note="Sulfite reductase [ferredoxin]"
FT /id="PRO_0000199953"
FT BINDING 446
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 452
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 491
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 495
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 495
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 52..137
FT /note="3'-(S-cysteinyl)-tyrosine (Tyr-Cys)"
FT /evidence="ECO:0000250"
FT CONFLICT 587
FT /note="R -> G (in Ref. 1; CAA77809)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 624 AA; 70131 MW; E5AABAFD6BBF4539 CRC64;
MSPTAAPQKL SKVEDLKARS QYLLEPILSQ LQEESTHFNE DGIQILKFHG SYQQDNRDNR
VKGQEKDFQF MLRLRSPGGY IPPQLYLTLD QLADDYGNGT LRATTRQAFQ LHGILKRDLK
TVIRRIVENL GSTISACGDV NRNVMAPPAP FRDRPEYEWA RTYANNIADL LTPESGAYYE
LWLDGEKVLS GEPDPAVLAA RRNPKGRVAD SVEPLYSDRY LPRKFKIAVT VPGDNSIDLF
TQDIGLVVIG NDRGELEGFN VYVGGGMGRT HNKEETFARL ADPLGFVPAA DIYAAVQAIV
ATQRDYGDRS NRRHARMKYL IHDWGIAKFK EAVESVFGKA IAPVRELPPF RYRDYLGWHE
QGDGKWFLGL PITSGRIKDD GNWQLRSALR EIVSRWQLPL LLTGSQDVLI YDVQPGDRAA
IDKLLRDRGV HTVEAIDSLQ RYAMACPALP TCGLAITESE RALPGLLVRI RRLLEEQGLP
DEHFVVRMTG CPNGCARPYM AELAFVGSAP NTYQLWLGGS PDQTRLARPF IDRLADGDVE
TQLRPLFVFF KQSRQAGESF GDFCDRVGFD ALRQFSESYQ HEAAKPRYRV GLRADVHGRL
KAEADKRGVS LTDLACEAIA AYLR
