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Database: UniProt
Entry: A0A1Z4LLI6_9CYAN
LinkDB: A0A1Z4LLI6_9CYAN
Original site: A0A1Z4LLI6_9CYAN 
ID   A0A1Z4LLI6_9CYAN        Unreviewed;        86 AA.
AC   A0A1Z4LLI6;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=sulfiredoxin {ECO:0000256|ARBA:ARBA00013055};
DE            EC=1.8.98.2 {ECO:0000256|ARBA:ARBA00013055};
GN   ORFNames=NIES267_15270 {ECO:0000313|EMBL:BAY82049.1};
OS   Calothrix parasitica NIES-267.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC   Calothrix.
OX   NCBI_TaxID=1973488 {ECO:0000313|EMBL:BAY82049.1, ECO:0000313|Proteomes:UP000218418};
RN   [1] {ECO:0000313|EMBL:BAY82049.1, ECO:0000313|Proteomes:UP000218418}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-267 {ECO:0000313|EMBL:BAY82049.1,
RC   ECO:0000313|Proteomes:UP000218418};
RA   Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT   "Genome sequencing of cyanobaciteial culture collection at National
RT   Institute for Environmental Studies (NIES).";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-dithiol + ATP + S-hydroxy-S-oxy-L-cysteinyl-
CC         [peroxiredoxin] = [protein]-disulfide + ADP + phosphate + S-hydroxy-
CC         L-cysteinyl-[peroxiredoxin]; Xref=Rhea:RHEA:17545, Rhea:RHEA-
CC         COMP:10593, Rhea:RHEA-COMP:10594, Rhea:RHEA-COMP:13681, Rhea:RHEA-
CC         COMP:17976, ChEBI:CHEBI:29950, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:50058, ChEBI:CHEBI:61973, ChEBI:CHEBI:61974,
CC         ChEBI:CHEBI:456216; EC=1.8.98.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00034024};
CC   -!- SIMILARITY: Belongs to the sulfiredoxin family.
CC       {ECO:0000256|ARBA:ARBA00009609}.
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DR   EMBL; AP018227; BAY82049.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z4LLI6; -.
DR   Proteomes; UP000218418; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0032542; F:sulfiredoxin activity; IEA:UniProtKB-EC.
DR   CDD; cd16395; Srx; 1.
DR   Gene3D; 3.90.1530.10; Conserved hypothetical protein from pyrococcus furiosus pfu- 392566-001, ParB domain; 1.
DR   InterPro; IPR003115; ParB/Sulfiredoxin_dom.
DR   InterPro; IPR036086; ParB/Sulfiredoxin_sf.
DR   InterPro; IPR016692; Sulfiredoxin.
DR   PANTHER; PTHR21348:SF2; SULFIREDOXIN-1; 1.
DR   PANTHER; PTHR21348; UNCHARACTERIZED; 1.
DR   Pfam; PF02195; ParBc; 1.
DR   PIRSF; PIRSF017267; Sulfiredoxin; 1.
DR   SMART; SM00470; ParB; 1.
DR   SUPFAM; SSF110849; ParB/Sulfiredoxin; 1.
PE   3: Inferred from homology;
KW   Antioxidant {ECO:0000256|ARBA:ARBA00022862};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          4..80
FT                   /note="ParB/Sulfiredoxin"
FT                   /evidence="ECO:0000259|SMART:SM00470"
SQ   SEQUENCE   86 AA;  9877 MW;  85C742EB0FA6B949 CRC64;
     MKVEEIPLNQ IIRPLPRQND SKKVEDLMKS IAEIGQQEPI DLLEVDGKYY GFSGCHRFEA
     CQRLGKETIK ARIRKAPKSV LKMHLA
//
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