ID A0A1Q3D2T8_CEPFO Unreviewed; 592 AA.
AC A0A1Q3D2T8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=assimilatory sulfite reductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012353};
DE EC=1.8.7.1 {ECO:0000256|ARBA:ARBA00012353};
DE Flags: Fragment;
GN ORFNames=CFOL_v3_30052 {ECO:0000313|EMBL:GAV86623.1};
OS Cephalotus follicularis (Albany pitcher plant).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Oxalidales; Cephalotaceae; Cephalotus.
OX NCBI_TaxID=3775 {ECO:0000313|EMBL:GAV86623.1, ECO:0000313|Proteomes:UP000187406};
RN [1] {ECO:0000313|Proteomes:UP000187406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. St1 {ECO:0000313|Proteomes:UP000187406};
RA Fukushima K., Hasebe M., Fang X.;
RT "Cephalotus genome sequencing.";
RL Submitted (APR-2016) 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=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:GAV86623.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BDDD01003976; GAV86623.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3D2T8; -.
DR STRING; 3775.A0A1Q3D2T8; -.
DR InParanoid; A0A1Q3D2T8; -.
DR OrthoDB; 5474937at2759; -.
DR Proteomes; UP000187406; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000187406};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 63..123
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 166..339
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT DOMAIN 357..410
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 436..573
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:GAV86623.1"
SQ SEQUENCE 592 AA; 67038 MW; 6B1DFE6D7847693D CRC64;
PIKPETAAET KRSKVEIIKE HSNFIRYPLN EELLTDAPNV NEAATQIIKF HGSYQQYNRD
ERGQRSYSFM LRTKNPSGKV PTQLYLTMDD LADEFGIGTL RLTTRTFQLH GVLKKDLKTV
ISSIIKNMGS TLGACGDLNR NVLAPAAPFA RKDYCFAQKT AEDIAALLSP QSGFYYDMWV
DGEKIMSAEP PEVVKARNDN SHGTNFPDSP EPIYGTQFLP RKFKVAVTVP TDNSVDILTN
DIGLVLVSDA QGEPQGFNIY VGGGMGRTHR VEATFPRLAE PLGYVPIEDI LYAVKAIVVT
QRENGRRDDR KYSRMKYLIS SWGIEKFRNV VEQYYGKKFE PFHELPEWEF KSYLGWHEQG
DGGLFCGFHV DNGRIGGKMK QTLREVIEKY NLSVRLTPNQ NIILCDIRGA WKRPITIALA
QAGLLHPRYV DPLNLTAMAC PAFPLCPLAI TEAERGIPVI LKRVRAVFEK VGLKFNESVV
IRITGCPNGC ARPYMAELGL VGDGPNSYQI WLGGTPNQTS LARSFMDKVK IQDLEKVFEP
LFYYWKRIRQ SKESFGDFTT RMGFEKLREW VDKWEGPEVA PARYNLKLFA DK
//
