ID A0A258FKR4_9CAUL Unreviewed; 219 AA.
AC A0A258FKR4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Alkyl hydroperoxide reductase C {ECO:0000256|ARBA:ARBA00017462};
DE EC=1.11.1.26 {ECO:0000256|ARBA:ARBA00013021};
DE AltName: Full=Peroxiredoxin {ECO:0000256|ARBA:ARBA00032077};
GN ORFNames=B7Z01_10610 {ECO:0000313|EMBL:OYX32608.1};
OS Brevundimonas subvibrioides.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=74313 {ECO:0000313|EMBL:OYX32608.1, ECO:0000313|Proteomes:UP000215595};
RN [1] {ECO:0000313|EMBL:OYX32608.1, ECO:0000313|Proteomes:UP000215595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32-69-9 {ECO:0000313|EMBL:OYX32608.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) 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|ARBA:ARBA00037420}.
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 -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009796}.
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:OYX32608.1}.
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DR EMBL; NCEB01000021; OYX32608.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A258FKR4; -.
DR Proteomes; UP000215595; Unassembled WGS sequence.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR PANTHER; PTHR10681:SF128; THIOREDOXIN-DEPENDENT PEROXIDE REDUCTASE, MITOCHONDRIAL; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 18..173
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 59
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 219 AA; 23722 MW; DF64E77C6D3063B8 CRC64;
MQTSDNAQPQ AVGSPRAVRL NDVAPDFTAR TTQGEKRLSD YRGRWLVLFS HPADFTPVCT
SEFIALARQA DGFAALGCDL LALSVDSLYS HLAWLKDIHQ RFGVKVPFPI IEDPSMAIGH
AFGMVDAGSS DSATVRATFV IDPDGIVRAI SWYPMNIGRS VDELLRLVTA LQVSDRDQAS
TPAGWSPGDP LLEPAATTLD DAIADGDGEA PWYYRERGA
//
