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Database: UniProt
Entry: A0A0W0V4P6_9GAMM
LinkDB: A0A0W0V4P6_9GAMM
Original site: A0A0W0V4P6_9GAMM 
ID   A0A0W0V4P6_9GAMM        Unreviewed;       182 AA.
AC   A0A0W0V4P6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
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_1 {ECO:0000313|EMBL:KTD15039.1};
GN   ORFNames=FOG18_12835 {ECO:0000313|EMBL:QDP73387.1}, Lisr_2384
GN   {ECO:0000313|EMBL:KTD15039.1};
OS   Legionella israelensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=454 {ECO:0000313|EMBL:KTD15039.1, ECO:0000313|Proteomes:UP000054761};
RN   [1] {ECO:0000313|EMBL:KTD15039.1, ECO:0000313|Proteomes:UP000054761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bercovier 4 {ECO:0000313|EMBL:KTD15039.1,
RC   ECO:0000313|Proteomes:UP000054761};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QDP73387.1, ECO:0000313|Proteomes:UP000320538}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L18-01051 {ECO:0000313|EMBL:QDP73387.1,
RC   ECO:0000313|Proteomes:UP000320538};
RA   Durieux I., Ginevra C., Attaiech L., Picq K., Juan P.A., Jarraud S.,
RA   Charpentier X.;
RT   "Diverse conjugative elements silence natural transformation in Legionella
RT   species.";
RL   Submitted (JUL-2019) 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};
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DR   EMBL; LNYH01000147; KTD15039.1; -; Genomic_DNA.
DR   EMBL; CP041668; QDP73387.1; -; Genomic_DNA.
DR   RefSeq; WP_058502673.1; NZ_UGOE01000002.1.
DR   AlphaFoldDB; A0A0W0V4P6; -.
DR   STRING; 454.Lisr_2384; -.
DR   PATRIC; fig|454.4.peg.2607; -.
DR   OrthoDB; 9812811at2; -.
DR   Proteomes; UP000054761; Unassembled WGS sequence.
DR   Proteomes; UP000320538; Chromosome.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054761}.
FT   DOMAIN          2..167
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        57
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT                   peroxidase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ   SEQUENCE   182 AA;  20262 MW;  4377984F20A2E050 CRC64;
     MLTVGQKLPE FSVVAVKPGF NHHEENGESA FETITDKSFA GKWKIIFFYP KDFTFVCPTE
     IVEFAKLNGE FADRDAVVLG GSTDNEFVKL AWRREHKDLY QLNQYSFADT QGQLTDGLGV
     RDVSAGVALR ATFIVDPENI IQHVSVNGLN VGRNPQEILR ILDALQTDEL CPCNRPVGGE
     TL
//
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