ID A0A086P6F9_SPHHM Unreviewed; 208 AA.
AC A0A086P6F9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=BV98_003377 {ECO:0000313|EMBL:KFG88977.1};
OS Sphingobium herbicidovorans (strain ATCC 700291 / DSM 11019 / NBRC 16415 /
OS MH) (Sphingomonas herbicidovorans).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1219045 {ECO:0000313|EMBL:KFG88977.1, ECO:0000313|Proteomes:UP000024284};
RN [1] {ECO:0000313|EMBL:KFG88977.1, ECO:0000313|Proteomes:UP000024284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 16415 {ECO:0000313|EMBL:KFG88977.1,
RC ECO:0000313|Proteomes:UP000024284};
RA Gan H.M., Gan H.Y., Savka M.A.;
RT "Draft genome sequences of Sphingobium herbicidovorans.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
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:KFG88977.1}.
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DR EMBL; JFZA02000045; KFG88977.1; -; Genomic_DNA.
DR RefSeq; WP_037468229.1; NZ_JFZA02000045.1.
DR AlphaFoldDB; A0A086P6F9; -.
DR STRING; 76947.GCA_002080435_03205; -.
DR PATRIC; fig|1219045.3.peg.3435; -.
DR eggNOG; COG0450; Bacteria.
DR Proteomes; UP000024284; 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:SF121; ALKYL HYDROPEROXIDE REDUCTASE C; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000024284}.
FT DOMAIN 13..168
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 54
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 208 AA; 22927 MW; 67C3F57232DC5E04 CRC64;
MSDDDTTCET GMLRIGDIAP DFRARSTQGD FQLSALRGQW VIFFSHPADF TPVCSTEFSA
LARRQAEFDA LGCTLVGLSV DSLYAHLAWV RALKDLFDVE IGFPIIEDPS MAVGRAYGMI
GDDAPDSMTM RSTFFIDPLG VIRATTCYPH NVGRSVDEML RLVRALQTVD AADRLTPEGW
VEGQPLLLPA ADRADAAADW FCRFEPKP
//
