ID A0A067F1P0_CITSI Unreviewed; 574 AA.
AC A0A067F1P0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 08-OCT-2025, entry version 31.
DE RecName: Full=assimilatory sulfite reductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012353};
DE EC=1.8.7.1 {ECO:0000256|ARBA:ARBA00012353};
GN ORFNames=CISIN_1g005564mg {ECO:0000313|EMBL:KDO61233.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO61233.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO61233.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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=hydrogen sulfide + 6 oxidized [2Fe-2S]-[ferredoxin] + 3 H2O =
CC sulfite + 6 reduced [2Fe-2S]-[ferredoxin] + 7 H(+);
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:ARBA00049518};
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 -!- SUBUNIT: Monomer. Interacts with ferredoxin.
CC {ECO:0000256|ARBA:ARBA00046513}.
CC -!- SUBCELLULAR LOCATION: 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}.
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DR EMBL; KK784926; KDO61233.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067F1P0; -.
DR SMR; A0A067F1P0; -.
DR Proteomes; UP000027120; Unassembled WGS sequence.
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 FunFam; 3.30.413.10:FF:000008; Sulfite reductase [ferredoxin], chloroplastic; 1.
DR FunFam; 3.90.480.10:FF:000001; Sulfite reductase [ferredoxin], chloroplastic; 1.
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; NF010029; PRK13504.1; 1.
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; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000027120};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 126..183
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 224..399
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT DOMAIN 417..480
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
SQ SEQUENCE 574 AA; 64489 MW; 023A3E8DAF4403AC CRC64;
MTTSFGAANT VIPNNPNIRI RSFNGLKPSH SLSIRTNLRA FPVPYASRSS VVRAVSTPVK
PETETKTETK RSKVEIIKEQ SNFIRYPLNE ELLTDAPNVN ESATQLIKFH GSYQQYNRDE
RGAKSYSFML RTKNPCGKVS NQLYLTMDDL ADQFGIGTLR LTTRQTFQLH GVLKKDLKTV
MRSIIRSMGS TLGACGDLNR NVLAPPAPLV RKDYLFAQKT AENIAALLTP QSGFYYDMWV
DGEQIMTAEP PEVVKARNDN SHGTNFPDSP EPIYGTQFLP RKFKVAVTVP TDNSVDILTN
DIGVVVVSDE NGEPQGFNLY VGGGMGRTHR LETTFPRLGE QLGYVPKEDI LYAVKAIVVT
QRENGRRDDR KYSRMKYLIS SWGIEKFRSV VEQYYGKKFE PFRQLPEWEF KSHLGWHEQG
DGGLFCGLHV DNGRIAGKMK KTLREIIEKY NLNVRITPNQ NIILCDIRKA WKRPITTALA
QAGLLLPRYV DPLNITAMAC PSLPLCPLAI TEAERGIPDI LKRIRAVFEK VGLKYNESVV
IRVTGCPNGC ARPYMAELGL VGDGPNSYQV FQLI
//
