GenomeNet

Database: UniProt
Entry: C0QBG5_DESAH
LinkDB: C0QBG5_DESAH
Original site: C0QBG5_DESAH 
ID   C0QBG5_DESAH            Unreviewed;       219 AA.
AC   C0QBG5;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 83.
DE   RecName: Full=Peroxiredoxin {ECO:0000256|HAMAP-Rule:MF_00401};
DE            EC=1.11.1.24 {ECO:0000256|HAMAP-Rule:MF_00401};
DE   AltName: Full=Thioredoxin peroxidase {ECO:0000256|HAMAP-Rule:MF_00401};
DE   AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000256|HAMAP-Rule:MF_00401};
GN   Name=ahpC {ECO:0000313|EMBL:ACN16967.1};
GN   OrderedLocusNames=HRM2_39090 {ECO:0000313|EMBL:ACN16967.1};
OS   Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS   HRM2) (Desulfobacterium autotrophicum).
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulforapulum.
OX   NCBI_TaxID=177437 {ECO:0000313|EMBL:ACN16967.1, ECO:0000313|Proteomes:UP000000442};
RN   [1] {ECO:0000313|EMBL:ACN16967.1, ECO:0000313|Proteomes:UP000000442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43914 / DSM 3382 / HRM2
RC   {ECO:0000313|Proteomes:UP000000442};
RX   PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA   Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA   Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA   Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA   Meyerdierks A., Gottschalk G., Amann R.;
RT   "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT   reducer oxidizing organic carbon completely to carbon dioxide.";
RL   Environ. Microbiol. 11:1038-1055(2009).
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|HAMAP-Rule:MF_00401}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC         disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC         COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC         ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00401};
CC   -!- SUBUNIT: Homodecamer. Pentamer of dimers that assemble into a ring
CC       structure. {ECO:0000256|HAMAP-Rule:MF_00401}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00401}.
CC   -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC       residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC       attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC       cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC       cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC       bridge. The disulfide is subsequently reduced by an appropriate
CC       electron donor to complete the catalytic cycle. Although the primary
CC       sequence of this enzyme is similar to those of the 1-Cys Prx6 enzymes,
CC       its catalytic properties resemble those of the typical 2-Cys Prxs and
CC       C(R) is provided by the other dimeric subunit to form an intersubunit
CC       disulfide. The disulfide is subsequently reduced by thioredoxin.
CC       {ECO:0000256|HAMAP-Rule:MF_00401}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC       {ECO:0000256|ARBA:ARBA00025719, ECO:0000256|HAMAP-Rule:MF_00401}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001087; ACN16967.1; -; Genomic_DNA.
DR   RefSeq; WP_015905710.1; NC_012108.1.
DR   AlphaFoldDB; C0QBG5; -.
DR   STRING; 177437.HRM2_39090; -.
DR   KEGG; dat:HRM2_39090; -.
DR   eggNOG; COG0450; Bacteria.
DR   HOGENOM; CLU_042529_4_4_7; -.
DR   OMA; RLTMLYP; -.
DR   OrthoDB; 9812811at2; -.
DR   Proteomes; UP000000442; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0140824; F:thioredoxin-dependent peroxiredoxin activity; IEA:UniProtKB-EC.
DR   CDD; cd03016; PRX_1cys; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   HAMAP; MF_00401; Peroxiredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR   InterPro; IPR022915; Peroxiredoxin_TDXH.
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; 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, ECO:0000256|HAMAP-
KW   Rule:MF_00401};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00401};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00401};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00401};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|HAMAP-
KW   Rule:MF_00401}; Redox-active center {ECO:0000256|HAMAP-Rule:MF_00401};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000442}.
FT   DOMAIN          9..163
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        51
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
FT   ACT_SITE        51
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT                   peroxidase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
FT   BINDING         126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
FT   DISULFID        51
FT                   /note="Interchain (with Cys-213); in linked form"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
FT   DISULFID        207..213
FT                   /note="Alternate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
FT   DISULFID        213
FT                   /note="Interchain (with Cys-51); in linked form"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
SQ   SEQUENCE   219 AA;  24863 MW;  A8E6EEB17E0B1042 CRC64;
     MEETKVNMPL LGDALPELKV QSTHGPMNIP GDMKGKWFVL FSHPADFTPV CTTEFVAFQK
     RYEEFEKLGC KLIGMSIDQV FSHIKWVQWI KAELDVDIKF PIVAANDSVA MKLGMLHPGK
     GTNTVRAVFI VDPDSKVRLI MYYPQEVGRN MDEIVRSVKA LQISDQQGAV AAGWPDNELI
     GDRIIMPPST NQADAEKRME KSDAFECFDW WFCHKPLEK
//
DBGET integrated database retrieval system