SIR_PEA
ID SIR_PEA Reviewed; 685 AA.
AC Q75NZ0; Q76KV3;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Sulfite reductase [ferredoxin], chloroplastic;
DE Short=PsSiR;
DE EC=1.8.7.1 {ECO:0000269|PubMed:11163356};
DE Flags: Precursor;
GN Name=SIR;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, PROTEIN SEQUENCE OF N-TERMINUS ANALYSIS, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Alaska;
RX PubMed=17371503; DOI=10.1111/j.1742-4658.2007.05748.x;
RA Sekine K., Fujiwara M., Nakayama M., Takao T., Hase T., Sato N.;
RT "DNA binding and partial nucleoid localization of the chloroplast stromal
RT enzyme ferredoxin:sulfite reductase.";
RL FEBS J. 274:2054-2069(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 377-685.
RC STRAIN=cv. Midoriusui; TISSUE=Epicotyl;
RX DOI=10.5511/plantbiotechnology.20.247;
RA Nakamura N., Marutani M., Sanematsu S., Toyoda K., Inagaki Y.-S.,
RA Shiraishi T., Ichinose Y.;
RT "Phylogenetic classification of Dof-type transcription factors in Pea
RT (Pisum sativum).";
RL Plant Biotechnol. 20:247-253(2003).
RN [3]
RP PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, SUBCELLULAR LOCATION, CATALYTIC
RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11163356; DOI=10.1016/s0014-5793(00)02342-5;
RA Sato N., Nakayama M., Hase T.;
RT "The 70-kDa major DNA-compacting protein of the chloroplast nucleoid is
RT sulfite reductase.";
RL FEBS Lett. 487:347-350(2001).
RN [4]
RP FUNCTION.
RX PubMed=11997391; DOI=10.1074/jbc.m201714200;
RA Sekine K., Hase T., Sato N.;
RT "Reversible DNA compaction by sulfite reductase regulates transcriptional
RT activity of chloroplast nucleoids.";
RL J. Biol. Chem. 277:24399-24404(2002).
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:0000269|PubMed:11163356, ECO:0000269|PubMed:11997391,
CC ECO:0000269|PubMed:17371503}.
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:0000269|PubMed:11163356, ECO:0000269|PubMed:11997391,
CC ECO:0000269|PubMed:17371503}.
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:0000269|PubMed:11163356};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=389 nm {ECO:0000269|PubMed:11163356,
CC ECO:0000269|PubMed:17371503};
CC Note=Exhibits a smaller absorbance peak at 580 nm. This absorption
CC spectrum indicates the presence of a siroheme-containing prosthetic
CC group.;
CC -!- SUBUNIT: Monomer. Interacts with ferredoxin (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma, chloroplast
CC nucleoid. Plastid, chloroplast stroma. Plastid stroma.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, and roots.
CC {ECO:0000269|PubMed:17371503}.
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; AB168112; BAD12837.2; -; mRNA.
DR EMBL; AB087846; BAC81658.1; -; mRNA.
DR AlphaFoldDB; Q75NZ0; -.
DR SMR; Q75NZ0; -.
DR MoonProt; Q75NZ0; -.
DR BRENDA; 1.8.7.1; 4872.
DR GO; GO:0042644; C:chloroplast nucleoid; IDA:UniProtKB.
DR GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IDA: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:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0019424; P:sulfide oxidation, using siroheme sulfite reductase; IDA: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; Thioether bond;
KW Transcription; Transcription regulation; Transit peptide.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:11163356,
FT ECO:0000269|PubMed:17371503"
FT CHAIN 52..685
FT /note="Sulfite reductase [ferredoxin], chloroplastic"
FT /id="PRO_5000181605"
FT BINDING 495
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 501
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 541
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 545
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 545
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 CONFLICT 586
FT /note="P -> L (in Ref. 2; BAC81658)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 685 AA; 76900 MW; 43CA953D71A9F77E CRC64;
MTTSFAAAAL RDPKLQIPNY HGLRSSSAAS SLSRNALSVP SSTRSSSLIR AVSTPAKSET
ATEKKRSKVE IFKEQSNFIR YPLNEDMLTD APNLSEAATQ LIKFHGSYQQ YNRDERGSRT
YSFMIRTKNP CGKVSNQLYL TMDDLADQFG IGTLRLTTRQ TFQLHGVVKK DLKTVMGSII
RNMGSSLGAC GDLNRNVLAP AAPIVSKDYL FAQETSENIA ALLTPQSGFY YDVWVDGERF
MSAEPPEVIQ ARNDNSHGTN FTDSPEPIYG TQFLPRKFKI AVTVPTDNSV DILTNDIGVV
VVTGDGGEPQ GFNLYVGGGM GRTHRMETTF PRLAEPLGYV PKEDILYAVK AIVVTQRENG
RRDDRRYSRM KYLIDSWGID KFRNVVEEYY GKKFEPFRSL PEWEFKSYLG WHQQGDGGLF
CGLHVDNGRI AGKMKTALRE VIEKYHLNVR LTPNQNLILT DIRAAWKRPI TTILSQAGLL
LPRYVDPLNI TAMACPAFPL CPLAITEAER GIPSILKRIR DMFEKVGLKY NESVVVRITG
CPNGCARPYM AELGLVGDGP NSYQIWLGGS SNQTSIARSF MDKVKPQDLE KVLEPLFYHW
KQKRQSKESF GDFTVRLGFE KLKEFIEKWE GPAVPPTRHN LKLFTDKDTY EAMDGLAKLQ
NKNAHQLAME VVRNYIASNL NGKGE
