ID   SIR2_MYCPA              Reviewed;         555 AA.
AC   Q73XV0;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Sulfite reductase [ferredoxin] 2;
DE            EC=1.8.7.1;
GN   Name=sir2; Synonyms=nirA2; OrderedLocusNames=MAP_2208;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016958; AAS04525.1; -; Genomic_DNA.
DR   RefSeq; WP_003878378.1; NC_002944.2.
DR   AlphaFoldDB; Q73XV0; -.
DR   SMR; Q73XV0; -.
DR   STRING; 262316.MAP_2208; -.
DR   PRIDE; Q73XV0; -.
DR   EnsemblBacteria; AAS04525; AAS04525; MAP_2208.
DR   KEGG; mpa:MAP_2208; -.
DR   PATRIC; fig|262316.17.peg.2348; -.
DR   eggNOG; COG0155; Bacteria.
DR   HOGENOM; CLU_015667_2_3_11; -.
DR   OMA; MGMTHGD; -.
DR   Proteomes; UP000000580; 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   Reference proteome; Thioether bond.
FT   CHAIN           1..555
FT                   /note="Sulfite reductase [ferredoxin] 2"
FT                   /id="PRO_0000199951"
FT   REGION          1..31
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;  61868 MW;  05317F4EEE477BF6 CRC64;
     MTTARPAKAR NEGQWALGNR EPLNPNEEMK QAGAPLAVRE RIETIYAKNG FDSIDKSDLR
     GRFRWWGLYT QREQGYDGSW TGDENIEKLE ARYFMMRVRC DGGAISAAAL RTLGQISVDF
     ARDTADITDR ENIQYHWIEV ENVPEIWRRL DAVGLRTTEA CGDCPRVILG SPLAGESLEE
     VIDPSWAIAE IARRYIGQPD FADLPRKYKT AISGLQDVAH EVNDVAFIGV NHPEHGPGLD
     LWVGGGLSTN PMLAQRVGAW VPLHEVPEVW AAVTSVFRDY GYRRLRSKAR LKFLVKDWGI
     EKFREVLETE YLKRPLIDGP APEPVAHPID HVGVQRLKNG LNAVGVAPIA GRVSGTILLA
     VADLAQQAGC DRIRFTPYQK LVLLDIPDDK LDEVVAGLEA LGLQSQPSHW RRNLMACSGI
     EFCKLSFAET RVRAQGLVPE LERRLADVNR QLDVPITINL NGCPNSCARI QVADIGLKGQ
     MVDDGEGGSV EGFQVHLGGS LGQDSGFGRK LRQHKVTSDE LGDYIERVAR NFVKYRGEGE
     RFAQWAMRAD EDDLR