ID Q18BV5_CLOD6 Unreviewed; 712 AA.
AC Q18BV5;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 113.
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=cotE {ECO:0000313|EMBL:CAJ68298.1};
GN OrderedLocusNames=CD630_14330 {ECO:0000313|EMBL:CAJ68298.1};
OS Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=272563 {ECO:0000313|EMBL:CAJ68298.1, ECO:0000313|Proteomes:UP000001978};
RN [1] {ECO:0000313|EMBL:CAJ68298.1, ECO:0000313|Proteomes:UP000001978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630 {ECO:0000313|EMBL:CAJ68298.1,
RC ECO:0000313|Proteomes:UP000001978};
RX PubMed=16804543; DOI=10.1038/ng1830;
RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA Price C., Rabbinowitsch R., Sharp S., Simmonds M., Steven K., Unwin L.,
RA Whithead S., Dupuy B., Dougan G., Barrell B.and.Parkhill.J.;
RT "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT mobile, mosaic genome.";
RL Nat. Genet. 38:779-786(2006).
RN [2] {ECO:0007829|PDB:6T9M, ECO:0007829|PDB:6TSB}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 348-712, AND DISULFIDE BONDS.
RX PubMed=32510464; DOI=10.1107/s2053230x20006147;
RA Whittingham J.L., Hanai S., Brannigan J.A., Ferreira W.T., Dodson E.J.,
RA Turkenburg J.P., Cartwright J., Cutting S.M., Wilkinson A.J.;
RT "Crystal structures of the GH18 domain of the bifunctional peroxiredoxin-
RT chitinase CotE from Clostridium difficile.";
RL Acta Crystallogr. F Struct. Biol. Commun. 76:241-249(2020).
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. AhpC/Prx1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009796}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC {ECO:0000256|ARBA:ARBA00025719, ECO:0000256|HAMAP-Rule:MF_00401}.
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DR EMBL; AM180355; CAJ68298.1; -; Genomic_DNA.
DR RefSeq; YP_001087934.1; NC_009089.1.
DR PDB; 6T9M; X-ray; 1.30 A; AAA=348-712.
DR PDB; 6TSB; X-ray; 2.10 A; AAA=348-712.
DR AlphaFoldDB; Q18BV5; -.
DR SMR; Q18BV5; -.
DR STRING; 272563.CD630_14330; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR EnsemblBacteria; CAJ68298; CAJ68298; CD630_14330.
DR KEGG; cdf:CD630_14330; -.
DR PATRIC; fig|272563.8.peg.1505; -.
DR eggNOG; COG0450; Bacteria.
DR eggNOG; COG3325; Bacteria.
DR OrthoDB; 9812811at2; -.
DR BioCyc; PDIF272563:G12WB-1571-MONOMER; -.
DR Proteomes; UP000001978; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0140824; F:thioredoxin-dependent peroxiredoxin activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd06548; GH18_chitinase; 1.
DR CDD; cd03016; PRX_1cys; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR HAMAP; MF_00401; Peroxiredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR022915; Peroxiredoxin_TDXH.
DR InterPro; IPR045020; PRX_1cys.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:6T9M, ECO:0007829|PDB:6TSB};
KW Antioxidant {ECO:0000256|ARBA:ARBA00022862, ECO:0000256|HAMAP-
KW Rule:MF_00401}; Capsid protein {ECO:0000313|EMBL:CAJ68298.1};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00401};
KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00401};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
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:UP000001978};
KW Virion {ECO:0000313|EMBL:CAJ68298.1}.
FT DOMAIN 8..163
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 377..698
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT ACT_SITE 49
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
FT DISULFID 49
FT /note="Interchain (with Cys-211); in linked form"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
FT DISULFID 205..211
FT /note="Alternate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
FT DISULFID 211
FT /note="Interchain (with Cys-49); in linked form"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
FT DISULFID 376..670
FT /evidence="ECO:0007829|PDB:6T9M, ECO:0007829|PDB:6TSB"
SQ SEQUENCE 712 AA; 81273 MW; FAC3A84F1589F884 CRC64;
MIYMPNLPSL GSKAPDFKAN TTNGPIRLSD YKGNWIVLFS HPGDFTPVCT TEFLCFAKYY
DEFKKRNTEL IGLSVDSNSS HLAWMYNISL LTGVEIPFPI IEDRDMRIAK LYGMISKPMS
DTSTVRSVFI IDNNQILRTI LYYPLTTGRN IPEILRIVDA LQTSDRDNIV TPANWFPGMP
VILPYPKNYK ELKNRVNSCN KKYSCMDWYL CFVPDNYNDE EVSKKIDNTC SWKKEHTKNI
ENECNCEHEH HDYLNKALDC KQEHKTDIKD DCNHEKKHTK NTNKVHNSKQ DKFKDKSCDE
MNFNYDKDES CDKINSSYNK EDSSYEDFYK HNYKNYDYTS EKNTKKIAMK TLKDSKKLVR
PQITDPYNPI VENANCPDIN PIVAEYVLGN PTNVDAQLLD AVIFAFAEID QSGNLFIPYP
RFLNQLLALK GEKPSLKVIV AIGGWGAEGF SDAALTPTSR YNFARQVNQM INEYALDGID
IDWEYPGSSA SGITSRPQDR ENFTLLLTAI RDVIGDDKWL SVAGTGDRGY INSSAEIDKI
APIIDYFNLM SYDFTAGETG PNGRKHQANL FDSDLSLPGY SVDAMVRNLE NAGMPSEKIL
LGIPFYGRLG ATITRTYDEL RRDYINKNGY EYRFDNTAQV PYLVKDGDFA MSYDDALSIF
LKTQYVLRNC LGGVFSWTST YDQANILART MSIGINDPEV LKEELEGIYG QF
//
