ID A0A199V7H2_ANACO Unreviewed; 128 AA.
AC A0A199V7H2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=sulfiredoxin {ECO:0000256|ARBA:ARBA00013055};
DE EC=1.8.98.2 {ECO:0000256|ARBA:ARBA00013055};
GN Name=LOC109704706 {ECO:0000313|RefSeq:XP_020081069.1};
GN ORFNames=ACMD2_07765 {ECO:0000313|EMBL:OAY72780.1};
OS Ananas comosus (Pineapple) (Ananas ananas).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Bromeliaceae;
OC Bromelioideae; Ananas.
OX NCBI_TaxID=4615 {ECO:0000313|EMBL:OAY72780.1, ECO:0000313|Proteomes:UP000092600};
RN [1] {ECO:0000313|EMBL:OAY72780.1, ECO:0000313|Proteomes:UP000092600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MD2 {ECO:0000313|Proteomes:UP000092600};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY72780.1};
RX PubMed=27374615; DOI=10.1093/dnares/dsw026;
RA Redwan R.M., Saidin A., Kumar S.V.;
RT "The draft genome of MD-2 pineapple using hybrid error correction of long
RT reads.";
RL DNA Res. 0:0-0(2016).
RN [2] {ECO:0000313|RefSeq:XP_020081069.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_020081069.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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; LSRQ01002987; OAY72780.1; -; Genomic_DNA.
DR RefSeq; XP_020081069.1; XM_020225480.1.
DR STRING; 4615.A0A199V7H2; -.
DR GeneID; 109704706; -.
DR OrthoDB; 5482730at2759; -.
DR Proteomes; UP000092600; Unassembled WGS sequence.
DR Proteomes; UP000515123; Unplaced.
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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000092600}.
FT DOMAIN 44..123
FT /note="ParB/Sulfiredoxin"
FT /evidence="ECO:0000259|SMART:SM00470"
SQ SEQUENCE 128 AA; 14280 MW; ACEE27D839DB9D19 CRC64;
MASPSLHFPP RIYTSSLSPI RASSNGRVPL PRGARSGGGG PAVVEIPLEQ IRRPLMRTRA
NDPAKVCQLM DSIRQIGLQE PIDVLEVDGV YYGFSGCHRF EAHQRLGLPT IRCKVRRGTK
ETLRHHMR
//
