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Database: UniProt
Entry: A0A2Z5G5B4_9BACT
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ID   A0A2Z5G5B4_9BACT        Unreviewed;       219 AA.
AC   A0A2Z5G5B4;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Alkyl hydroperoxide reductase subunit C-like protein {ECO:0000313|EMBL:AXC14170.1};
GN   ORFNames=ACPOL_4908 {ECO:0000313|EMBL:AXC14170.1};
OS   Acidisarcina polymorpha.
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Acidisarcina.
OX   NCBI_TaxID=2211140 {ECO:0000313|EMBL:AXC14170.1, ECO:0000313|Proteomes:UP000253606};
RN   [1] {ECO:0000313|EMBL:AXC14170.1, ECO:0000313|Proteomes:UP000253606}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SBC82 {ECO:0000313|EMBL:AXC14170.1,
RC   ECO:0000313|Proteomes:UP000253606};
RX   PubMed=30510549; DOI=10.3389/fmicb.2018.02775;
RA   Belova S.E., Ravin N.V., Pankratov T.A., Rakitin A.L., Ivanova A.A.,
RA   Beletsky A.V., Mardanov A.V., Sinninghe Damste J.S., Dedysh S.N.;
RT   "Hydrolytic Capabilities as a Key to Environmental Success: Chitinolytic
RT   and Cellulolytic Acidobacteria From Acidic Sub-arctic Soils and Boreal
RT   Peatlands.";
RL   Front. Microbiol. 9:2775-2775(2018).
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00009796}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC       {ECO:0000256|ARBA:ARBA00025719}.
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DR   EMBL; CP030840; AXC14170.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z5G5B4; -.
DR   KEGG; abas:ACPOL_4908; -.
DR   OrthoDB; 9812811at2; -.
DR   Proteomes; UP000253606; Chromosome.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR   CDD; cd03016; PRX_1cys; 1.
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; IPR045020; PRX_1cys.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR43503; MCG48959-RELATED; 1.
DR   PANTHER; PTHR43503:SF4; PEROXIREDOXIN-6; 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.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Antioxidant {ECO:0000256|ARBA:ARBA00022862};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253606}.
FT   DOMAIN          3..168
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        45
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT                   peroxidase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ   SEQUENCE   219 AA;  24385 MW;  3E3FF3DCCD4B7313 CRC64;
     MSLRINDIAP DFTAETTQGT IHFHEWIGDG WAVLFSHPKD FTPVCTTELG SVAGLYPEFQ
     KRHCKVIGLS VDPVSSHGKW AVDIEETQGH RVDYPMIGDP ELKIAKLYDM LPADAGASSE
     GRTAANNATV RTVFIIGPDK RIKLQLSYPM STGRNFPEIL RVLDSMQLTA KHKVATPANW
     QQGEDVIILP SVSDEEAREK YADGWKTVKP YLRIVPQPQ
//
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