SIR1_TOBAC
ID SIR1_TOBAC Reviewed; 693 AA.
AC O82802;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Sulfite reductase 1 [ferredoxin], chloroplastic;
DE Short=NtSiR1;
DE EC=1.8.7.1;
DE Flags: Precursor;
GN Name=SIR1;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 63-72, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. SR1; TISSUE=Leaf;
RX PubMed=9722674; DOI=10.1093/oxfordjournals.jbchem.a022156;
RA Yonekura-Sakakibara K., Ashikari T., Tanaka Y., Kusumi T., Hase T.;
RT "Molecular characterization of tobacco sulfite reductase: enzyme
RT purification, gene cloning, and gene expression analysis.";
RL J. Biochem. 124:615-621(1998).
CC -!- FUNCTION: Essential protein with sulfite reductase activity required in
CC assimilatory sulfate reduction pathway during both primary and
CC secondary metabolism and thus involved in development and growth.
CC {ECO:0000250|UniProtKB:Q75NZ0}.
CC -!- FUNCTION: DNA-binding protein that binds to both double-stranded and
CC single-stranded DNA without significant sequence specificity to
CC reversibly repress the transcriptional activity of chloroplast
CC nucleoids by promoting DNA compaction and possibly regulate DNA
CC replication. {ECO:0000250|UniProtKB:Q75NZ0}.
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:Q75NZ0};
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. Interacts with ferredoxin (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma, chloroplast nucleoid
CC {ECO:0000250}. Plastid, chloroplast stroma {ECO:0000250}. Plastid
CC stroma {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, roots and petals.
CC {ECO:0000269|PubMed:9722674}.
CC -!- PTM: Phosphorylated; this phosphorylation reduces DNA-binding.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC family. {ECO:0000305}.
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DR EMBL; D83583; BAA33531.1; -; mRNA.
DR EMBL; AB010717; BAA33796.1; -; Genomic_DNA.
DR PIR; JE0260; JE0260.
DR RefSeq; NP_001312233.1; NM_001325304.1.
DR AlphaFoldDB; O82802; -.
DR SMR; O82802; -.
DR STRING; 4097.O82802; -.
DR PRIDE; O82802; -.
DR GeneID; 107780886; -.
DR KEGG; nta:107780886; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0042644; C:chloroplast nucleoid; ISS:UniProtKB.
DR GO; GO:0009570; C:chloroplast stroma; ISS:UniProtKB.
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:0003677; F:DNA binding; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0016002; F:sulfite reductase activity; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0000103; P:sulfate assimilation; IBA:GO_Central.
DR GO; GO:0019424; P:sulfide oxidation, using siroheme sulfite reductase; ISS:UniProtKB.
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; Chloroplast; Direct protein sequencing; DNA-binding; Heme; Iron;
KW Iron-sulfur; Metal-binding; Oxidoreductase; Plastid; Reference proteome;
KW Thioether bond; Transit peptide.
FT TRANSIT 1..62
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:9722674"
FT CHAIN 63..693
FT /note="Sulfite reductase 1 [ferredoxin], chloroplastic"
FT /id="PRO_0000416845"
FT BINDING 502
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 508
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 548
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 552
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 552
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"
SQ SEQUENCE 693 AA; 77963 MW; F93F365E9AD816C4 CRC64;
MTTSFGAAIN IAVADDPNPK LQIHNFSGLK STSNSLLLSR RLHVFQSFSP SNPSSIVRAV
STPAKPAAVE PKRSKVEIFK EQSNFIRYPL NEEILNDAPN INEAATQLIK FHGSYMQYDR
DERGGRSYSF MLRTKNPGGE VPNRLYLVMD DLADQFGIGT LRLTTRQTFQ LHGVLKKNLK
TVMSTIIKNM GSTLGACGDL NRNVLAPAAP FAKKDYMFAK QTADNIAALL TPQSGFYYDV
WVDGEKVMTA EPPEVVKARN DNSHGTNFPD SPEPIYGTQF LPRKFKIAVT VPTDNSVDIF
TNDIGVVVVS NEDGEPQGFN IYVGGGMGRT HRMETTFPRL AEPLGYVPKE DILYAVKAIV
VTQRENGRRD DRRYSRLKYL LSSWGIEKFR SVTEQYYGKK FQPCRELPEW EFKSYLGWHE
AGDGSLFCGL HVDNGRVKGA MKKALREVIE KYNLNVRLTP NQNIILCNIR QAWKRPITTV
LAQGGLLQPR YVDPLNLTAM ACPAFPLCPL AITEAERGIP DILKRVRAIF ERVGLKYSES
VVIRITGCPN GCARPYMAEL GLVGDGPNSY QIWLGGTPNQ TSLAKTFKDK LKVQDLEKVL
EPLFFHWRRK RQSKESFGDF TNRMGFEKLG EFVEKWEGIP ESSSRYNLKL FADRETYEAM
DALASIQDKN AHQLAIEVVR NYVASQQNGK SMD
