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Sulfite reductase [ferredoxin], chloroplastic (GmSiR) (EC 1.8.7.1) (Nucleoid DNA-compacting protein of 68 kDa) (Fragment)

 SIR_SOYBN               Reviewed;         573 AA.
Q9AWB2;
18-APR-2012, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
12-SEP-2018, entry version 74.
RecName: Full=Sulfite reductase [ferredoxin], chloroplastic;
Short=GmSiR;
EC=1.8.7.1;
AltName: Full=Nucleoid DNA-compacting protein of 68 kDa;
Flags: Precursor; Fragment;
Name=SIR; Synonyms=DCP68;
Glycine max (Soybean) (Glycine hispida).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
50 kb inversion clade; NPAAA clade; indigoferoid/millettioid clade;
Phaseoleae; Glycine; Soja.
NCBI_TaxID=3847;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Keaton M.A., Cannon G.C., Heinhorst S.;
"cDNA sequence for soybean ferredoxin:sulfite reductase.";
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
[2]
PROTEIN SEQUENCE OF 55-69, FUNCTION, SUBCELLULAR LOCATION,
BIOPHYSICOCHEMICAL PROPERTIES, AND PHOSPHORYLATION.
PubMed=12081370; DOI=10.1023/A:1015500431421;
Chi-Ham C.L., Keaton M.A., Cannon G.C., Heinhorst S.;
"The DNA-compacting protein DCP68 from soybean chloroplasts is
ferredoxin:sulfite reductase and co-localizes with the organellar
nucleoid.";
Plant Mol. Biol. 49:621-631(2002).
[3]
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=10350096; DOI=10.1023/A:1006135615924;
Cannon G.C., Ward L.N., Case C.I., Heinhorst S.;
"The 68 kDa DNA compacting nucleoid protein from soybean chloroplasts
inhibits DNA synthesis in vitro.";
Plant Mol. Biol. 39:835-845(1999).
-!- FUNCTION: Essential protein with sulfite reductase activity
required in assimilatory sulfate reduction pathway during both
primary and secondary metabolism and thus involved in development
and growth. {ECO:0000269|PubMed:12081370}.
-!- FUNCTION: DNA-binding protein that binds to both double-stranded
and single-stranded DNA without significant sequence specificity
to reversibly repress the transcriptional activity of chloroplast
nucleoids by promoting DNA compaction and possibly regulate DNA
replication. {ECO:0000269|PubMed:10350096}.
-!- CATALYTIC ACTIVITY: Hydrogen sulfide + 6 oxidized ferredoxin
[iron-sulfur] cluster + 3 H(2)O = sulfite + 6 reduced ferredoxin
[iron-sulfur] cluster + 6 H(+). {ECO:0000250|UniProtKB:Q75NZ0}.
-!- COFACTOR:
Name=siroheme; Xref=ChEBI:CHEBI:60052; Evidence={ECO:0000250};
Note=Binds 1 siroheme per subunit. {ECO:0000250};
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Note=Binds 1 [4Fe-4S] cluster per subunit.;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Absorption:
Abs(max)=386 nm {ECO:0000269|PubMed:12081370};
Note=Exhibits a smaller absorbance peak at 587 nm. This
absorption spectrum indicates the presence of a siroheme-
containing prosthetic group.;
-!- SUBUNIT: Monomer. Interacts with ferredoxin (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma, chloroplast
nucleoid. Plastid, chloroplast stroma. Plastid stroma
{ECO:0000250}.
-!- PTM: Phosphorylated; this phosphorylation reduces DNA-binding.
{ECO:0000269|PubMed:12081370}.
-!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S
domain family. {ECO:0000305}.
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EMBL; AY017473; AAG59996.1; -; mRNA.
UniGene; Gma.4906; -.
ProteinModelPortal; Q9AWB2; -.
SMR; Q9AWB2; -.
STRING; 3847.GLYMA11G09890.1; -.
PRIDE; Q9AWB2; -.
ProMEX; Q9AWB2; -.
eggNOG; KOG0560; Eukaryota.
eggNOG; COG0155; LUCA.
InParanoid; Q9AWB2; -.
Proteomes; UP000008827; Unplaced.
GO; GO:0042644; C:chloroplast nucleoid; IDA:UniProtKB.
GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0050311; F:sulfite reductase (ferredoxin) activity; ISS:UniProtKB.
GO; GO:0016002; F:sulfite reductase activity; IBA:GO_Central.
GO; GO:0006323; P:DNA packaging; IDA:UniProtKB.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:1900160; P:plastid DNA packaging; IDA:UniProtKB.
GO; GO:0006275; P:regulation of DNA replication; IDA:UniProtKB.
GO; GO:0019419; P:sulfate reduction; IBA:GO_Central.
GO; GO:0019424; P:sulfide oxidation, using siroheme sulfite reductase; IDA:UniProtKB.
InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
InterPro; IPR036136; Nit/Sulf_reduc_fer_like_dom_sf.
InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
InterPro; IPR011787; SiR_ferredoxin-dep.
Pfam; PF01077; NIR_SIR; 2.
Pfam; PF03460; NIR_SIR_ferr; 2.
PRINTS; PR00397; SIROHAEM.
SUPFAM; SSF55124; SSF55124; 2.
TIGRFAMs; TIGR02042; sir; 1.
PROSITE; PS00365; NIR_SIR; 1.
1: Evidence at protein level;
4Fe-4S; Chloroplast; Complete proteome; Direct protein sequencing;
DNA replication; DNA-binding; Heme; Iron; Iron-sulfur; Metal-binding;
Oxidoreductase; Phosphoprotein; Plastid; Reference proteome;
Thioether bond; Transit peptide.
TRANSIT 1 54 Chloroplast.
{ECO:0000269|PubMed:12081370}.
CHAIN 55 >573 Sulfite reductase [ferredoxin],
chloroplastic.
/FTId=PRO_0000416846.
METAL 497 497 Iron-sulfur (4Fe-4S). {ECO:0000250}.
METAL 503 503 Iron-sulfur (4Fe-4S). {ECO:0000250}.
METAL 543 543 Iron-sulfur (4Fe-4S). {ECO:0000250}.
METAL 547 547 Iron (siroheme axial ligand).
{ECO:0000250}.
METAL 547 547 Iron-sulfur (4Fe-4S). {ECO:0000250}.
NON_TER 573 573
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


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