SIR_SOYBN
ID SIR_SOYBN Reviewed; 573 AA.
AC Q9AWB2;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Sulfite reductase [ferredoxin], chloroplastic;
DE Short=GmSiR;
DE EC=1.8.7.1;
DE AltName: Full=Nucleoid DNA-compacting protein of 68 kDa;
DE Flags: Precursor; Fragment;
GN Name=SIR; Synonyms=DCP68;
OS Glycine max (Soybean) (Glycine hispida).
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; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Keaton M.A., Cannon G.C., Heinhorst S.;
RT "cDNA sequence for soybean ferredoxin:sulfite reductase.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 55-69, FUNCTION, SUBCELLULAR LOCATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND PHOSPHORYLATION.
RX PubMed=12081370; DOI=10.1023/a:1015500431421;
RA Chi-Ham C.L., Keaton M.A., Cannon G.C., Heinhorst S.;
RT "The DNA-compacting protein DCP68 from soybean chloroplasts is
RT ferredoxin:sulfite reductase and co-localizes with the organellar
RT nucleoid.";
RL Plant Mol. Biol. 49:621-631(2002).
RN [3]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=10350096; DOI=10.1023/a:1006135615924;
RA Cannon G.C., Ward L.N., Case C.I., Heinhorst S.;
RT "The 68 kDa DNA compacting nucleoid protein from soybean chloroplasts
RT inhibits DNA synthesis in vitro.";
RL Plant Mol. Biol. 39:835-845(1999).
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:12081370}.
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:10350096}.
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;
CC Note=Binds 1 [4Fe-4S] cluster per subunit.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=386 nm {ECO:0000269|PubMed:12081370};
CC Note=Exhibits a smaller absorbance peak at 587 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 {ECO:0000250}.
CC -!- PTM: Phosphorylated; this phosphorylation reduces DNA-binding.
CC {ECO:0000269|PubMed:12081370}.
CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC family. {ECO:0000305}.
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DR EMBL; AY017473; AAG59996.1; -; mRNA.
DR AlphaFoldDB; Q9AWB2; -.
DR SMR; Q9AWB2; -.
DR STRING; 3847.GLYMA11G09890.1; -.
DR PRIDE; Q9AWB2; -.
DR ProMEX; Q9AWB2; -.
DR eggNOG; KOG0560; Eukaryota.
DR InParanoid; Q9AWB2; -.
DR Proteomes; UP000008827; Unplaced.
DR GO; GO:0042644; C:chloroplast nucleoid; IDA:UniProtKB.
DR GO; GO:0009570; C:chloroplast stroma; IDA: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; 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:0016002; F:sulfite reductase activity; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:1900160; P:plastid chromosome packaging; IDA:UniProtKB.
DR GO; GO:0000103; P:sulfate assimilation; IBA:GO_Central.
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 replication;
KW DNA-binding; Heme; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW Phosphoprotein; Plastid; Reference proteome; Thioether bond;
KW Transit peptide.
FT TRANSIT 1..54
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:12081370"
FT CHAIN 55..>573
FT /note="Sulfite reductase [ferredoxin], chloroplastic"
FT /id="PRO_0000416846"
FT BINDING 497
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 503
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 543
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 547
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 547
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 NON_TER 573
SQ SEQUENCE 573 AA; 63822 MW; FD02A907B746B2D9 CRC64;
MTTSFGPATT SAPLKDHKVQ IPSFHGLRSS SASALPRNAL SLPSSTRSLS LIRAVSTPAQ
SETATVKRSK VEIFKEQSNF IRYPLNEDIL TDAPNISEAA TQLIKFHGSY QQYNREERGS
RSYSFMIRTK NPCGKVSNQL YLTMDDLADQ FGIGTLRLTT RQTFQLHGVL KKDLKTVMGT
IIRNMGSTLG ACGDLNRNVL APAAPLARKD YLFAQQTAEN IAALLAPQSG FYYDIWVDGE
KILTSEPPEV VQARNDNSHG TNFPDSPEPI YGTQFLPRKF KIAVTVPTDN SVDILTNDIG
VVVVTDDDGE PQGFNIYVGG GMGRTHRLET TFPRLAEPIG YVPKEDILYA VKAIVVTQRE
NGRRDDRKYS RLKYLISSWG IEKFRSVVEQ YYGKKFEPFR ALPEWEFKSY LGWHEQGDGK
LFYGLHVDNG RIGGNMKKTL REVIEKYNLN VRITPNQNII LTDVRAAWKR PITTTLAQAG
LLQPRFVDPL NITAMACPAF PLCPLAITEA ERGIPNILKR IRDVFDKVGL KYSESVVVRI
TGCPNGCARP YMAELGLVGD GPNSYQIWLG GTP
