ID A0A0X8G5K1_9FLAO Unreviewed; 236 AA.
AC A0A0X8G5K1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Peroxiredoxin {ECO:0000256|HAMAP-Rule:MF_00401};
DE EC=1.11.1.24 {ECO:0000256|HAMAP-Rule:MF_00401};
DE AltName: Full=Thioredoxin peroxidase {ECO:0000256|HAMAP-Rule:MF_00401};
DE AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000256|HAMAP-Rule:MF_00401};
GN ORFNames=Lupro_01855 {ECO:0000313|EMBL:AMC10073.1};
OS Lutibacter profundi.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Lutibacter.
OX NCBI_TaxID=1622118 {ECO:0000313|EMBL:AMC10073.1, ECO:0000313|Proteomes:UP000059672};
RN [1] {ECO:0000313|Proteomes:UP000059672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LP1 {ECO:0000313|Proteomes:UP000059672};
RA Wissuwa J., Le Moine Bauer S., Stokke R., Dahle H., Steen I.H.;
RT "Complete genome sequence of Lutibacter profundus strain LP1.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMC10073.1, ECO:0000313|Proteomes:UP000059672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LP1 {ECO:0000313|EMBL:AMC10073.1,
RC ECO:0000313|Proteomes:UP000059672};
RX PubMed=27118569; DOI=10.1099/ijsem.0.001105;
RA Le Moine Bauer S., Roalkvam I., Steen I.H., Dahle H.;
RT "Lutibacter profundi sp. nov., isolated from a deep-sea hydrothermal system
RT on the Arctic Mid-Ocean Ridge and emended description of the genus
RT Lutibacter.";
RL Int. J. Syst. Evol. Microbiol. 66:2671-2677(2016).
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. {ECO:0000256|HAMAP-Rule:MF_00401}.
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00401};
CC -!- SUBUNIT: Homodecamer. Pentamer of dimers that assemble into a ring
CC structure. {ECO:0000256|HAMAP-Rule:MF_00401}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00401}.
CC -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC bridge. The disulfide is subsequently reduced by an appropriate
CC electron donor to complete the catalytic cycle. Although the primary
CC sequence of this enzyme is similar to those of the 1-Cys Prx6 enzymes,
CC its catalytic properties resemble those of the typical 2-Cys Prxs and
CC C(R) is provided by the other dimeric subunit to form an intersubunit
CC disulfide. The disulfide is subsequently reduced by thioredoxin.
CC {ECO:0000256|HAMAP-Rule:MF_00401}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009796}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC {ECO:0000256|ARBA:ARBA00025719, ECO:0000256|HAMAP-Rule:MF_00401}.
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; CP013355; AMC10073.1; -; Genomic_DNA.
DR RefSeq; WP_068205791.1; NZ_CP013355.1.
DR AlphaFoldDB; A0A0X8G5K1; -.
DR STRING; 1622118.Lupro_01855; -.
DR KEGG; lut:Lupro_01855; -.
DR PATRIC; fig|1622118.3.peg.378; -.
DR OrthoDB; 9812811at2; -.
DR Proteomes; UP000059672; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0140824; F:thioredoxin-dependent peroxiredoxin activity; IEA:UniProtKB-EC.
DR CDD; cd03016; PRX_1cys; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR HAMAP; MF_00401; Peroxiredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR022915; Peroxiredoxin_TDXH.
DR InterPro; IPR045020; PRX_1cys.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10681:SF171; AT16346P-RELATED; 1.
DR PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR Pfam; PF10417; 1-cysPrx_C; 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 3: Inferred from homology;
KW Antioxidant {ECO:0000256|ARBA:ARBA00022862, ECO:0000256|HAMAP-
KW Rule:MF_00401};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00401};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP-
KW Rule:MF_00401};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00401};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|HAMAP-
KW Rule:MF_00401}; Redox-active center {ECO:0000256|HAMAP-Rule:MF_00401};
KW Reference proteome {ECO:0000313|Proteomes:UP000059672}.
FT DOMAIN 11..173
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 53
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
FT ACT_SITE 53
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
FT DISULFID 53
FT /note="Interchain (with Cys-220); in linked form"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
FT DISULFID 214..220
FT /note="Alternate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
FT DISULFID 220
FT /note="Interchain (with Cys-53); in linked form"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
SQ SEQUENCE 236 AA; 26628 MW; 02002D9E5B17DC94 CRC64;
METQQEFTSM PRIGDKAPEF KAVTTQGDIN FPSDYNGGWS ILFSHPADFT PVCTSEFITF
ASLEDKFKEA NCSLIGLSID GLYSHIAWLR SIKEKIEYKG MKNVDVKFPL IEDITMEIAK
KYGMLQPNED STKAVRAVFF VDPKGIIRTI IYYPLSLGRN FDELYRVLIA LQAADAFDIA
TPADWRPGDD VIIGPAGSCG TAKDRMEGKE DMDCKDWYFC TKKISKEEIL SKVLKK
//
