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Database: UniProt
Entry: A0A3N2QMA2_9RHOB
LinkDB: A0A3N2QMA2_9RHOB
Original site: A0A3N2QMA2_9RHOB 
ID   A0A3N2QMA2_9RHOB        Unreviewed;       233 AA.
AC   A0A3N2QMA2;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
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=EAT49_18885 {ECO:0000313|EMBL:ROT96304.1};
OS   Histidinibacterium lentulum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Histidinibacterium.
OX   NCBI_TaxID=2480588 {ECO:0000313|EMBL:ROT96304.1, ECO:0000313|Proteomes:UP000268016};
RN   [1] {ECO:0000313|EMBL:ROT96304.1, ECO:0000313|Proteomes:UP000268016}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B17 {ECO:0000313|EMBL:ROT96304.1,
RC   ECO:0000313|Proteomes:UP000268016};
RA   Wang G.;
RT   "Histidinibacterium lentulum gen. nov., sp. nov., a marine bacterium from
RT   the culture broth of Picochlorum sp. 122.";
RL   Submitted (OCT-2018) 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:ROT96304.1}.
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DR   EMBL; RDRB01000012; ROT96304.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N2QMA2; -.
DR   OrthoDB; 9812811at2; -.
DR   Proteomes; UP000268016; Unassembled WGS sequence.
DR   GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
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   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000268016}.
FT   DOMAIN          29..185
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   233 AA;  26462 MW;  F3862F12C339889E CRC64;
     MKRALFSRKK RTTVADVPTS YRTTVRWLPK IGDYVPNFRA ETTMGPLTFH PWAEGLWTVL
     FSHPKAFTPV CTTEVAAMAA MHDEFRRRGV QILGLCASSL EEQLTWHHEI AQLFGHRVRF
     PMISDVDGEL ARLIGMVHGK EHEDWPIRKT LIIDPSLKVR AITEYPMVVG RSSEETLRLI
     DALQRVTAFR VVTGADWEKG DRVMLHPGVD APPTLFARQV RPYLVACDDP MAS
//
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