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
//