ID U5BVY9_9BACT Unreviewed; 162 AA.
AC U5BVY9;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Peroxiredoxin {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=P872_03690 {ECO:0000313|EMBL:ERM80102.1};
OS Rhodonellum psychrophilum GCM71 = DSM 17998.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC Rhodonellum.
OX NCBI_TaxID=1123057 {ECO:0000313|EMBL:ERM80102.1, ECO:0000313|Proteomes:UP000016843};
RN [1] {ECO:0000313|EMBL:ERM80102.1, ECO:0000313|Proteomes:UP000016843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GCM71 {ECO:0000313|EMBL:ERM80102.1,
RC ECO:0000313|Proteomes:UP000016843};
RX PubMed=24309741;
RA Hauptmann A.L., Glaring M.A., Hallin P.F., Prieme A., Stougaard P.;
RT "Draft Genome Sequence of the Psychrophilic and Alkaliphilic Rhodonellum
RT psychrophilum Strain GCM71T.";
RL Genome Announc. 1:e01014-13(2013).
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides. {ECO:0000256|ARBA:ARBA00037420}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009796}.
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:ERM80102.1}.
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DR EMBL; AWXR01000192; ERM80102.1; -; Genomic_DNA.
DR RefSeq; WP_022582431.1; NZ_AWXR01000192.1.
DR AlphaFoldDB; U5BVY9; -.
DR PATRIC; fig|1123057.7.peg.5104; -.
DR eggNOG; COG0450; Bacteria.
DR OrthoDB; 9812811at2; -.
DR Proteomes; UP000016843; Unassembled WGS sequence.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR PANTHER; PTHR10681:SF128; THIOREDOXIN-DEPENDENT PEROXIDE REDUCTASE, MITOCHONDRIAL; 1.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000016843}.
FT DOMAIN 1..89
FT /note="Alkyl hydroperoxide reductase subunit C/ Thiol
FT specific antioxidant"
FT /evidence="ECO:0000259|Pfam:PF00578"
FT DOMAIN 110..145
FT /note="Peroxiredoxin C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10417"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ERM80102.1"
SQ SEQUENCE 162 AA; 18469 MW; 4A477F96926C5733 CRC64;
TEMTGFALNQ DFFDEKNTKL VGLSIDSIHS HIAWVNNVKK NTGVLFEFPI IADIDMKVSK
LYGMLQPGES ETAAVRAVFF IDPKGKIRLV MYYPLNVGRN MDEIKRALIA LQTSDKHKVS
LPLDWREGDK VIVSPPKTVK EMLEREASDY EMVDFYLAKK DL
//
