ID Q9PER7_XYLFA Unreviewed; 159 AA.
AC Q9PER7;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 133.
DE RecName: Full=thioredoxin-dependent peroxiredoxin {ECO:0000256|ARBA:ARBA00013017};
DE EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
DE AltName: Full=Bacterioferritin comigratory protein {ECO:0000256|ARBA:ARBA00041373};
DE AltName: Full=Thioredoxin peroxidase {ECO:0000256|ARBA:ARBA00032824};
DE AltName: Full=Thioredoxin-dependent peroxiredoxin Bcp {ECO:0000256|ARBA:ARBA00042639};
GN OrderedLocusNames=XF_0961 {ECO:0000313|EMBL:AAF83771.1};
OS Xylella fastidiosa (strain 9a5c).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=160492 {ECO:0000313|EMBL:AAF83771.1, ECO:0000313|Proteomes:UP000000812};
RN [1] {ECO:0000313|EMBL:AAF83771.1, ECO:0000313|Proteomes:UP000000812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9a5c {ECO:0000313|EMBL:AAF83771.1,
RC ECO:0000313|Proteomes:UP000000812};
RX PubMed=10910347; DOI=10.1038/35018003;
RA Simpson A.J., Reinach F.C., Arruda P., Abreu F.A., Acencio M.,
RA Alvarenga R., Alves L.M., Araya J.E., Baia G.S., Baptista C.S.,
RA Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.,
RA Bueno M.R., Camargo A.A., Camargo L.E., Carraro D.M., Carrer H.,
RA Colauto N.B., Colombo C., Costa F.F., Costa M.C., Costa-Neto C.M.,
RA Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H.,
RA Facincani A.P., Ferreira A.J., Ferreira V.C., Ferro J.A., Fraga J.S.,
RA Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H.,
RA Goldman M.H., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D.,
RA Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E.,
RA Laigret F., Lambais M.R., Leite L.C., Lemos E.G., Lemos M.V., Lopes S.A.,
RA Lopes C.R., Machado J.A., Machado M.A., Madeira A.M., Madeira H.M.,
RA Marino C.L., Marques M.V., Martins E.A., Martins E.M., Matsukuma A.Y.,
RA Menck C.F., Miracca E.C., Miyaki C.Y., Monteriro-Vitorello C.B., Moon D.H.,
RA Nagai M.A., Nascimento A.L., Netto L.E., Nhani A.Jr., Nobrega F.G.,
RA Nunes L.R., Oliveira M.A., de Oliveira M.C., de Oliveira R.C.,
RA Palmieri D.A., Paris A., Peixoto B.R., Pereira G.A., Pereira H.A.Jr.,
RA Pesquero J.B., Quaggio R.B., Roberto P.G., Rodrigues V., de M Rosa A.J.,
RA de Rosa V.E.Jr., de Sa R.G., Santelli R.V., Sawasaki H.E., da Silva A.C.,
RA da Silva A.M., da Silva F.R., da Silva W.A.Jr., da Silveira J.F.,
RA Silvestri M.L., Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F.,
RA Truffi D., Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A.,
RA Verjovski-Almeida S., Vettore A.L., Zago M.A., Zatz M., Meidanis J.,
RA Setubal J.C.;
RT "The genome sequence of the plant pathogen Xylella fastidiosa.";
RL Nature 406:151-159(2000).
RN [2] {ECO:0007829|PDB:3IXR}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS).
RA Horta B.B., Oliveira M.A., Discola K.F., Cussiol J.R.R., Netto L.E.S.;
RT "Biochemical and Structural Analysis Indicates that PrxQ, a Cys Based
RT Peroxidase from Xylella fastidiosa, possesses high reactivity towards
RT hydroperoxides.";
RL Submitted (SEP-2009) to the PDB data bank.
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides and as sensor of hydrogen peroxide-mediated
CC signaling events. {ECO:0000256|ARBA:ARBA00003330}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.24;
CC Evidence={ECO:0000256|ARBA:ARBA00000280};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. BCP/PrxQ subfamily.
CC {ECO:0000256|ARBA:ARBA00038489}.
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DR EMBL; AE003849; AAF83771.1; -; Genomic_DNA.
DR PIR; B82742; B82742.
DR RefSeq; WP_010893480.1; NC_002488.3.
DR PDB; 3IXR; X-ray; 1.60 A; A=1-159.
DR PDBsum; 3IXR; -.
DR AlphaFoldDB; Q9PER7; -.
DR SMR; Q9PER7; -.
DR STRING; 160492.XF_0961; -.
DR KEGG; xfa:XF_0961; -.
DR PATRIC; fig|160492.11.peg.1028; -.
DR eggNOG; COG1225; Bacteria.
DR HOGENOM; CLU_042529_14_1_6; -.
DR BRENDA; 1.11.1.24; 6734.
DR EvolutionaryTrace; Q9PER7; -.
DR Proteomes; UP000000812; Chromosome.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd03017; PRX_BCP; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR42801:SF24; PEROXIREDOXIN BCP; 1.
DR PANTHER; PTHR42801; THIOREDOXIN-DEPENDENT PEROXIDE REDUCTASE; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:3IXR};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 1..158
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 47
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 159 AA; 17813 MW; 6174CA90F9A1F8A1 CRC64;
MNIGDTLNHS LLNHPLMLSG STCKTLSDYT NQWLVLYFYP KDNTPGCSTE GLEFNLLLPQ
FEQINATVLG VSRDSVKSHD SFCAKQGFTF PLVSDSDAIL CKAFDVIKEK TMYGRQVIGI
ERSTFLIGPT HRIVEAWRQV KVPGHAEEVL NKLKAHAEQ
//
