ID A0A0C9NDQ2_SPHPI Unreviewed; 181 AA.
AC A0A0C9NDQ2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
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 Name=ahpC {ECO:0000313|EMBL:GAN12868.1};
GN ORFNames=SP6_14_00240 {ECO:0000313|EMBL:GAN12868.1};
OS Sphingomonas paucimobilis NBRC 13935.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1219050 {ECO:0000313|EMBL:GAN12868.1, ECO:0000313|Proteomes:UP000032025};
RN [1] {ECO:0000313|EMBL:GAN12868.1, ECO:0000313|Proteomes:UP000032025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 13935 {ECO:0000313|EMBL:GAN12868.1,
RC ECO:0000313|Proteomes:UP000032025};
RA Hosoyama A., Hashimoto M., Hosoyama Y., Noguchi M., Uohara A., Ohji S.,
RA Katano-Makiyama Y., Ichikawa N., Kimura A., Yamazoe A., Fujita N.;
RT "Whole genome shotgun sequence of Sphingomonas paucimobilis NBRC 13935.";
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 -!- 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:GAN12868.1}.
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DR EMBL; BBJS01000014; GAN12868.1; -; Genomic_DNA.
DR RefSeq; WP_007403328.1; NZ_BBJS01000014.1.
DR AlphaFoldDB; A0A0C9NDQ2; -.
DR GeneID; 78529377; -.
DR Proteomes; UP000032025; Unassembled WGS sequence.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd03015; PRX_Typ2cys; 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; PTHR10681:SF121; ALKYL HYDROPEROXIDE REDUCTASE C; 1.
DR PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 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 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 2..161
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 51
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 181 AA; 19924 MW; 531F5F7C20C7D743 CRC64;
MLTVGDKLPA FTVPVQQGTN ALPAGETISD TSYEGKWKVL FYWPKDFTFV CPTEIVGYAQ
LKDDFADRDA VLIGASTDTA HVHLAWRKSD PDLAAADFPW IADNGRVLAD ALGIVDKNEH
VAYRATFIID PDNVIQHVTI NGLNVGRNPQ ETLRVLDALQ TDELCPCNWN KGDDVLQLAA
E
//
