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Database: UniProt
Entry: A0A165JY91_9BURK
LinkDB: A0A165JY91_9BURK
Original site: A0A165JY91_9BURK 
ID   A0A165JY91_9BURK        Unreviewed;       202 AA.
AC   A0A165JY91;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Alkyl hydroperoxide reductase {ECO:0000313|EMBL:KZT14820.1};
GN   ORFNames=A1D30_16645 {ECO:0000313|EMBL:KZT14820.1};
OS   Acidovorax sp. GW101-3H11.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=1813946 {ECO:0000313|EMBL:KZT14820.1, ECO:0000313|Proteomes:UP000077219};
RN   [1] {ECO:0000313|Proteomes:UP000077219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GW101-3H11 {ECO:0000313|Proteomes:UP000077219};
RA   Ray J., Price M., Deutschbauer A.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KZT14820.1, ECO:0000313|Proteomes:UP000077219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GW101-3H11 {ECO:0000313|EMBL:KZT14820.1,
RC   ECO:0000313|Proteomes:UP000077219};
RX   PubMed=29769716; DOI=10.1038/s41586-018-0124-0;
RA   Price M.N., Wetmore K.M., Waters R.J., Callaghan M., Ray J., Liu H.,
RA   Kuehl J.V., Melnyk R.A., Lamson J.S., Suh Y., Carlson H.K., Esquivel Z.,
RA   Sadeeshkumar H., Chakraborty R., Zane G.M., Rubin B.E., Wall J.D.,
RA   Visel A., Bristow J., Blow M.J., Arkin A.P., Deutschbauer A.M.;
RT   "Mutant phenotypes for thousands of bacterial genes of unknown function.";
RL   Nature 557:503-509(2018).
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:KZT14820.1}.
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DR   EMBL; LUKZ01000014; KZT14820.1; -; Genomic_DNA.
DR   RefSeq; WP_063461605.1; NZ_LUKZ01000014.1.
DR   AlphaFoldDB; A0A165JY91; -.
DR   STRING; 1813946.A1D30_16645; -.
DR   OrthoDB; 9781543at2; -.
DR   Proteomes; UP000077219; Unassembled WGS sequence.
DR   GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd02969; PRX_like1; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR047262; PRX-like1.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR43640; OS07G0260300 PROTEIN; 1.
DR   PANTHER; PTHR43640:SF1; THIOREDOXIN-DEPENDENT PEROXIREDOXIN; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..202
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007860399"
FT   DOMAIN          23..175
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   202 AA;  21410 MW;  44216686F447E5EF CRC64;
     MKLLRRTLIA TATLVALGAQ AATAVGQPAP DFTLKDTSGK TVRLSDFKGK HVVLEWTNPG
     CPFVRKHYDS GNMPATQKDA TSKGVVWLSI NSTEKASSDY LEPAKLAAWK TERKSASTAV
     LMDEEGTVGK SYGARTTPHM YIVNPQGMLV YAGGIDSIPS ARPADIEKAT NYVTVGLGEA
     LAGKPISAAT TAPYGCSIKY KS
//
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