ID A0A2P6QFL1_ROSCH Unreviewed; 688 AA.
AC A0A2P6QFL1;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=assimilatory sulfite reductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012353};
DE EC=1.8.7.1 {ECO:0000256|ARBA:ARBA00012353};
GN ORFNames=RchiOBHm_Chr5g0052341 {ECO:0000313|EMBL:PRQ32975.1};
OS Rosa chinensis (China rose).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Rosoideae; Rosoideae incertae sedis;
OC Rosa.
OX NCBI_TaxID=74649 {ECO:0000313|EMBL:PRQ32975.1, ECO:0000313|Proteomes:UP000238479};
RN [1] {ECO:0000313|EMBL:PRQ32975.1, ECO:0000313|Proteomes:UP000238479}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Old Blush {ECO:0000313|Proteomes:UP000238479};
RA Bendahmane M.;
RT "The Rosa genome provides new insights in the design of modern roses.";
RL Nat. Genet. 0:0-0(2018).
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:0000256|ARBA:ARBA00002010}.
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:0000256|ARBA:ARBA00003329}.
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:0000256|ARBA:ARBA00000993};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- COFACTOR:
CC Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC Evidence={ECO:0000256|ARBA:ARBA00001929};
CC -!- SUBCELLULAR LOCATION: Plastid stroma {ECO:0000256|ARBA:ARBA00004646}.
CC Plastid, chloroplast stroma, chloroplast nucleoid
CC {ECO:0000256|ARBA:ARBA00004595}.
CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC family. {ECO:0000256|ARBA:ARBA00010429}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PRQ32975.1}.
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DR EMBL; PDCK01000043; PRQ32975.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P6QFL1; -.
DR STRING; 74649.A0A2P6QFL1; -.
DR EnsemblPlants; PRQ32975; PRQ32975; RchiOBHm_Chr5g0052341.
DR Gramene; PRQ32975; PRQ32975; RchiOBHm_Chr5g0052341.
DR OMA; RNVMAPA; -.
DR OrthoDB; 5474937at2759; -.
DR Proteomes; UP000238479; Chromosome 5.
DR GO; GO:0042644; C:chloroplast nucleoid; IEA:UniProtKB-SubCell.
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; Sulfite Reductase Hemoprotein, domain 1; 2.
DR Gene3D; 3.90.480.10; Sulfite Reductase Hemoprotein;Domain 2; 1.
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 NCBIfam; TIGR02042; sir; 1.
DR PANTHER; PTHR11493:SF47; SULFITE REDUCTASE [NADPH] SUBUNIT BETA; 1.
DR PANTHER; PTHR11493; SULFITE REDUCTASE [NADPH] SUBUNIT BETA-RELATED; 1.
DR Pfam; PF01077; NIR_SIR; 2.
DR Pfam; PF03460; NIR_SIR_ferr; 2.
DR PRINTS; PR00397; SIROHAEM.
DR SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 2.
DR SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 2.
DR PROSITE; PS00365; NIR_SIR; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:PRQ32975.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000238479};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 124..179
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 221..395
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT DOMAIN 415..468
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 494..631
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
SQ SEQUENCE 688 AA; 77561 MW; 7D9EE1B02105EB91 CRC64;
MTTTTATAAA VLREPKVEIG RYQGLRSANS LALTAGGRHV TLFNASSRSS SLIRAVSTPA
KPETVTKRSK VEIFKEQSNF IRYPLNEEIL TDTPNINEAA TQLIKFHGSY QQYNRDERGG
RSYSFMLRTK NPCGKVSNQL YLTMDDLADQ FGIGTLRLTT RQTFQLHGVL KKDLKTVMSS
IIRSMGSTLG ACGDLNRNVL APAAPLLRKD YLFAQKTAEN IAALLTPQSG FYYDVWVDGE
QFLTAEPPEV TKVRNDNSNG KTFTDSPEPI YGTQFLPRKF KIAVTVPTDN SVDILTNDIG
VVVVTDDNGE PQGFNIYVGG GMGRTHRLES TFARLAEPLG YVPKEDILKA IKSIVEVQRD
HGRRDDRKYS RMKYLISDWG IEKFRRELED NYYQKKFEPF RKLPEWEFKS YLGWHEQGDG
SLFCGLHVDN GRIGGKMKKA LREVISKYNL SIRLTPNQNI ILCDIRNAWK RPITTTLAQA
GLLHPRYVDP LNQTAMACPA FPLCPLAITE AERGIPDILK RVRAVFEKVG LKYNESVVIR
VTGCPNGCAR PYMAELGLVG DGPNSYQIWL GGTPNQTSIA KTFMNKVKVQ DLEKVFEPLF
YHWKRKRQAK ESFGDFTIRM GFEKLQVLVD KWEGPEVAPT RYNLKLFADK ETYEAVDELA
KLQGKSAHQL AMEVIRNFVA SQQNGKSE
//
