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Database: UniProt
Entry: A0A388L5L0_CHABU
LinkDB: A0A388L5L0_CHABU
Original site: A0A388L5L0_CHABU 
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
//
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