ID A0A388L5L0_CHABU Unreviewed; 745 AA.
AC A0A388L5L0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=assimilatory sulfite reductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012353};
DE EC=1.8.7.1 {ECO:0000256|ARBA:ARBA00012353};
GN ORFNames=CBR_g23983 {ECO:0000313|EMBL:GBG77538.1};
OS Chara braunii (Braun's stonewort).
OC Eukaryota; Viridiplantae; Streptophyta; Charophyceae; Charales; Characeae;
OC Chara.
OX NCBI_TaxID=69332 {ECO:0000313|EMBL:GBG77538.1, ECO:0000313|Proteomes:UP000265515};
RN [1] {ECO:0000313|EMBL:GBG77538.1, ECO:0000313|Proteomes:UP000265515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S276 {ECO:0000313|EMBL:GBG77538.1,
RC ECO:0000313|Proteomes:UP000265515};
RX PubMed=30007417; DOI=10.1016/j.cell.2018.06.033;
RA Nishiyama T., Sakayama H., Vries J.D., Buschmann H., Saint-Marcoux D.,
RA Ullrich K.K., Haas F.B., Vanderstraeten L., Becker D., Lang D.,
RA Vosolsobe S., Rombauts S., Wilhelmsson P.K.I., Janitza P., Kern R.,
RA Heyl A., Rumpler F., Villalobos L.I.A.C., Clay J.M., Skokan R., Toyoda A.,
RA Suzuki Y., Kagoshima H., Schijlen E., Tajeshwar N., Catarino B.,
RA Hetherington A.J., Saltykova A., Bonnot C., Breuninger H., Symeonidi A.,
RA Radhakrishnan G.V., Van Nieuwerburgh F., Deforce D., Chang C., Karol K.G.,
RA Hedrich R., Ulvskov P., Glockner G., Delwiche C.F., Petrasek J.,
RA Van de Peer Y., Friml J., Beilby M., Dolan L., Kohara Y., Sugano S.,
RA Fujiyama A., Delaux P.-M., Quint M., TheiBen G., Hagemann M., Harholt J.,
RA Dunand C., Zachgo S., Langdale J., Maumus F., Straeten D.V.D., Gould S.B.,
RA Rensing S.A.;
RT "The Chara Genome: Secondary Complexity and Implications for Plant
RT Terrestrialization.";
RL Cell 174:448-464(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:GBG77538.1}.
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DR EMBL; BFEA01000270; GBG77538.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A388L5L0; -.
DR STRING; 69332.A0A388L5L0; -.
DR EnsemblPlants; GBG77538; GBG77538; CBR_g23983.
DR Gramene; GBG77538; GBG77538; CBR_g23983.
DR OMA; WQMMLRL; -.
DR Proteomes; UP000265515; Unassembled WGS sequence.
DR GO; GO:0042644; C:chloroplast nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0010319; C:stromule; IEA:EnsemblPlants.
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 GO; GO:0016002; F:sulfite reductase activity; IEA:EnsemblPlants.
DR GO; GO:0009409; P:response to cold; IEA:EnsemblPlants.
DR GO; GO:0006790; P:sulfur compound metabolic process; IEA:EnsemblPlants.
DR Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 2.
DR Gene3D; 3.90.480.10; Sulfite Reductase Hemoprotein;Domain 2; 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 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:UP000265515};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 221..279
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 321..500
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT DOMAIN 520..572
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
SQ SEQUENCE 745 AA; 83137 MW; 065C8539FE9BCE9B CRC64;
MLCLNWLGST RRLDSPQLDS ARVDSARVDF ARVDFTRVDS ARADSARADS ARVDFARFDS
ARFDSAHVDS VLLDSPLLES AHGSNRLGSN RLGSVRVSSA RLGSTQLGSA RLSSAQLVDW
AHYKWQIYNA AGDVNSFLKY DHISANAVRI KHQPKTPPTT GPAKRNKVEI YKENSGFLRH
PLIEEMQTEA KGINDAAAQI IKFHGTYLQD NREERTFGGE KPYQFMIRTK QPAGKVTNSV
YLLMDKLADE FGIGTLRLTT RQTFQLHGIL KKDLKTVLST IIRNFGSTIG TCGDLNRNTL
APPAPFKNDP AYLYAQEYAE KIATLLAPQA GSYYEVWVDD EKFMSAEMAR ETEDVKIARA
DNSHGTNFEG SLEPIYGTQF LPRKFKIAVT APGDNSVDIL TNDIGLVTIT DENGQLQGFD
IFVGGGMGRT HRNSATFPLL AQPLGFVAKD DVLYAVKAIV ATQRDYGRRD DRRQARMKYL
VNEWGIDKFR TVVEQYFGKP LEPFKELPPW EFRHYLGWHE QGDGLLFLGV HVENGRVKGD
AKKALRDVIA EFDIPIRLMA NQNIILCDIQ PSWKSKIQLT LSEAGLVEPQ DVDDLNLTAM
ACPALPLCPL AVTEAERVMP DTLKRVRTVL NKVGLRNPSD AMVIRMTGCP NGCTRPYMAE
LAFVGDGPSS YQVYLGGSRN QTRLAKLFMD KMKAQNLETT LEPVFYMYKT QRLTGDGEPE
TFGDFADRVG FEAIHSYMAG YGGME
//