SIR1_MYCPA
ID SIR1_MYCPA Reviewed; 555 AA.
AC Q73YC1;
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] 1;
DE EC=1.8.7.1;
GN Name=sir1; Synonyms=nirA1; OrderedLocusNames=MAP_2035;
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}.
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DR EMBL; AE016958; AAS04352.1; -; Genomic_DNA.
DR RefSeq; WP_003878226.1; NC_002944.2.
DR AlphaFoldDB; Q73YC1; -.
DR SMR; Q73YC1; -.
DR STRING; 262316.MAP_2035; -.
DR PRIDE; Q73YC1; -.
DR EnsemblBacteria; AAS04352; AAS04352; MAP_2035.
DR KEGG; mpa:MAP_2035; -.
DR PATRIC; fig|262316.17.peg.2157; -.
DR eggNOG; COG0155; Bacteria.
DR HOGENOM; CLU_015667_2_3_11; -.
DR OMA; IKISGCM; -.
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] 1"
FT /id="PRO_0000199950"
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; 62149 MW; 747EBFAD163B8206 CRC64;
MTTARPVKTR NEGQWALGDR EPLNDTEKIK LADGPLNVRE RIINVYAKQG FDSIDKSDLR
GRFRWMGLYT QREQGYDGSW TGDDNTDKIE AKYFMMRVRS DGKAMSAHTM RTLGQISTEF
ARDTADISDR ENLQLHWIRI EDVPEIWRRL ESVGLQTTEA CGDCPRGIHG SPLAGDSLDE
VLDPSPAIEE IVRRSLNNPE YANLPRKYKT AVSGLQDVSH ETHDVAFVGV EHPEHGPGLD
LWVGGGLSTN PMLAQRLSVW VPLDEVPDVW EAVTQLFRDY GYRRLRAKAR LKFLVKDWGI
EKFREILEQE YLNRRLIDGP APAPVKHTID HVGVQKIKNG LNAVGVAPIA GRVSGTTLSA
VADLMEQVGS DRARWTPFQK LVILDVPDDK VDELVTGLDA LGLPSRPSSW RKNTMACTGI
EFCKLSFAET RVRTQTLVPE LERRLADVDA QLDAPISVHL NGCPNSCARI QVADIGFKGQ
WIDNGDGTSV EGFQVHLGGG LGEQSGFGRK LRQHKVTSEE LGDYIDRVTR KYLEGRNDGE
TFASWALRAD EEELR
