(data stored in ACNUC7421 zone)

SWISSPROT: C8W4V6_DESAS

ID   C8W4V6_DESAS            Unreviewed;       226 AA.
AC   C8W4V6;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 52.
DE   RecName: Full=Peroxiredoxin {ECO:0000256|HAMAP-Rule:MF_00401};
DE            EC=1.11.1.15 {ECO:0000256|HAMAP-Rule:MF_00401};
DE   AltName: Full=Thioredoxin peroxidase {ECO:0000256|HAMAP-Rule:MF_00401};
GN   OrderedLocusNames=Dtox_0355 {ECO:0000313|EMBL:ACV61308.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61308.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61308.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction
CC       of hydrogen peroxide and organic hydroperoxides to water and
CC       alcohols, respectively. Plays a role in cell protection against
CC       oxidative stress by detoxifying peroxides. {ECO:0000256|HAMAP-
CC       Rule:MF_00401}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-dithiol + a hydroperoxide = [protein]-disulfide
CC         + an alcohol + H2O; Xref=Rhea:RHEA:10008, Rhea:RHEA-COMP:10593,
CC         Rhea:RHEA-COMP:10594, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058;
CC         EC=1.11.1.15; Evidence={ECO:0000256|HAMAP-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
CC       cysteine residue, the peroxidatic cysteine (C(P)), which makes the
CC       nucleophilic attack on the peroxide substrate. The peroxide
CC       oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which
CC       then reacts with another cysteine residue, the resolving cysteine
CC       (C(R)), to form a disulfide bridge. The disulfide is subsequently
CC       reduced by an appropriate electron donor to complete the catalytic
CC       cycle. Although the primary sequence of this enzyme is similar to
CC       those of the 1-Cys Prx6 enzymes, its catalytic properties resemble
CC       those of the typical 2-Cys Prxs and C(R) is provided by the other
CC       dimeric subunit to form an intersubunit disulfide. The disulfide
CC       is subsequently reduced by thioredoxin. {ECO:0000256|HAMAP-
CC       Rule:MF_00401}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00401}.
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DR   EMBL; CP001720; ACV61308.1; -; Genomic_DNA.
DR   STRING; 485916.Dtox_0355; -.
DR   EnsemblBacteria; ACV61308; ACV61308; Dtox_0355.
DR   KEGG; dae:Dtox_0355; -.
DR   eggNOG; ENOG4105D3R; Bacteria.
DR   eggNOG; COG0450; LUCA.
DR   HOGENOM; HOG000022346; -.
DR   KO; K03386; -.
DR   OMA; YPIIADD; -.
DR   BioCyc; DACE485916:G1GFV-371-MONOMER; -.
DR   Proteomes; UP000002217; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   HAMAP; MF_00401; Peroxiredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR   InterPro; IPR019479; Peroxiredoxin_C.
DR   InterPro; IPR022915; Peroxiredoxin_TDXH.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF10417; 1-cysPrx_C; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   PIRSF; PIRSF000239; AHPC; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8W4V6.
DR   SWISS-2DPAGE; C8W4V6.
KW   Antioxidant {ECO:0000256|HAMAP-Rule:MF_00401};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00401};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00401};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00401,
KW   ECO:0000313|EMBL:ACV61308.1};
KW   Peroxidase {ECO:0000256|HAMAP-Rule:MF_00401,
KW   ECO:0000313|EMBL:ACV61308.1};
KW   Redox-active center {ECO:0000256|HAMAP-Rule:MF_00401};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217}.
FT   DOMAIN       11    173       Thioredoxin. {ECO:0000259|PROSITE:
FT                                PS51352}.
FT   ACT_SITE     53     53       Cysteine sulfenic acid (-SOH)
FT                                intermediate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00401, ECO:0000256|PIRSR:PIRSR000239-
FT                                1}.
FT   BINDING     136    136       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00401}.
FT   DISULFID     53     53       Interchain (with Cys-221); in linked
FT                                form. {ECO:0000256|HAMAP-Rule:MF_00401}.
FT   DISULFID    215    221       Alternate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00401}.
FT   DISULFID    221    221       Interchain (with Cys-53); in linked form.
FT                                {ECO:0000256|HAMAP-Rule:MF_00401}.
SQ   SEQUENCE   226 AA;  25595 MW;  F36EB269B06F6D8B CRC64;
     MDSMSESFRM PLIGDDAPVF TAKTTMGDIN FPADYKGKWV IFFSHPADFT PVCTTEFMTF
     ATMQEELKKL NTELIGLSID SIYAHIAWLR TIKDKIEYKG MKNVEVLFPL IEDLKMDVAK
     KFGMVQPNAS TTQAVRAVFI IDPNSKVRAI LYYPLTTGRN MEEIKRMIIA MQKSDSDGVA
     TPANWVPGDD VIIPPPGSCG SAKERMESQE EGKYCLDWFM CFRKEK
//

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