ID A0A095SA14_9GAMM Unreviewed; 239 AA.
AC A0A095SA14;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=T9A_01430 {ECO:0000313|EMBL:KGD61481.1};
OS Alcanivorax jadensis T9.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alcanivorax.
OX NCBI_TaxID=1177181 {ECO:0000313|EMBL:KGD61481.1, ECO:0000313|Proteomes:UP000029443};
RN [1] {ECO:0000313|EMBL:KGD61481.1, ECO:0000313|Proteomes:UP000029443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T9 {ECO:0000313|EMBL:KGD61481.1,
RC ECO:0000313|Proteomes:UP000029443};
RA Lai Q., Shao Z.;
RT "Genome Sequence of alkane-degrading Bacterium Alcanivorax jadensis T9.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a hydroperoxide + H(+) + NADH = an alcohol + H2O + NAD(+);
CC Xref=Rhea:RHEA:62628, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.11.1.26;
CC Evidence={ECO:0000256|ARBA:ARBA00000318};
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 -!- 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:KGD61481.1}.
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DR EMBL; ARXU01000004; KGD61481.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A095SA14; -.
DR STRING; 1177181.T9A_01430; -.
DR PATRIC; fig|1177181.3.peg.1431; -.
DR eggNOG; COG0450; Bacteria.
DR Proteomes; UP000029443; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0102039; F:NADH-dependent peroxiredoxin activity; IEA:RHEA.
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; 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 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}.
FT DOMAIN 34..189
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 75
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
FT DISULFID 75
FT /note="Interchain (with Cys-235); in linked form"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
FT DISULFID 229..235
FT /note="Alternate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
FT DISULFID 235
FT /note="Interchain (with Cys-75); in linked form"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
SQ SEQUENCE 239 AA; 26520 MW; 696D0FA093D05183 CRC64;
MEYINAHSLV MNFTTLEPTE IAMDMNNQTQ SGLPRINEPA PDFTALTTDG EKSLSDYRGK
WLVLFSHPAD FTPVCTTEFM AFAKAAPEFA KRNCELLGLS IDSIHSHIAW MRNIKQNFGV
EIPFPIIEDL KMNVANAYGM IHPGAADTSA VRATFIIDPN GVLRAMVYYP MSNGRSIPEF
LRLLEALQTS DENGVATPEG WQPGDKVIVP PAKTAEAANQ RVESGEYECT DFYFCTKSL
//
