ID   SIR_MYCTO               Reviewed;         555 AA.
AC   P9WJ02; L0T9H3; P71753; Q7D781;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Sulfite reductase [ferredoxin];
DE            EC=1.8.7.1;
GN   Name=sir; Synonyms=nirA; OrderedLocusNames=MT2461;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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   -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC       family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK46756.1; -; Genomic_DNA.
DR   PIR; B70682; B70682.
DR   RefSeq; WP_003899303.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WJ02; -.
DR   SMR; P9WJ02; -.
DR   EnsemblBacteria; AAK46756; AAK46756; MT2461.
DR   GeneID; 45426377; -.
DR   KEGG; mtc:MT2461; -.
DR   HOGENOM; CLU_015667_2_3_11; -.
DR   Proteomes; UP000001020; 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: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; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR   InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
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   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..555
FT                   /note="Sulfite reductase [ferredoxin]"
FT                   /id="PRO_0000427915"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         417
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         423
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         463
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         467
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         467
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        69..161
FT                   /note="3'-(S-cysteinyl)-tyrosine (Tyr-Cys)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   555 AA;  62112 MW;  68925CA37C131BC3 CRC64;
     MTTARPAKAR NEGQWALGHR EPLNANEELK KAGNPLDVRE RIENIYAKQG FDSIDKTDLR
     GRFRWWGLYT QREQGYDGTW TGDDNIDKLE AKYFMMRVRC DGGALSAAAL RTLGQISTEF
     ARDTADISDR QNVQYHWIEV ENVPEIWRRL DDVGLQTTEA CGDCPRVVLG SPLAGESLDE
     VLDPTWAIEE IVRRYIGKPD FADLPRKYKT AISGLQDVAH EINDVAFIGV NHPEHGPGLD
     LWVGGGLSTN PMLAQRVGAW VPLGEVPEVW AAVTSVFRDY GYRRLRAKAR LKFLIKDWGI
     AKFREVLETE YLKRPLIDGP APEPVKHPID HVGVQRLKNG LNAVGVAPIA GRVSGTILTA
     VADLMARAGS DRIRFTPYQK LVILDIPDAL LDDLIAGLDA LGLQSRPSHW RRNLMACSGI
     EFCKLSFAET RVRAQHLVPE LERRLEDINS QLDVPITVNI NGCPNSCARI QIADIGFKGQ
     MIDDGHGGSV EGFQVHLGGH LGLDAGFGRK LRQHKVTSDE LGDYIDRVVR NFVKHRSEGE
     RFAQWVIRAE EDDLR