TPX_HAEIN
ID TPX_HAEIN Reviewed; 165 AA.
AC Q57549;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Thiol peroxidase {ECO:0000255|HAMAP-Rule:MF_00269};
DE Short=Tpx {ECO:0000255|HAMAP-Rule:MF_00269};
DE EC=1.11.1.24 {ECO:0000255|HAMAP-Rule:MF_00269, ECO:0000269|PubMed:9141476};
DE AltName: Full=Peroxiredoxin tpx {ECO:0000255|HAMAP-Rule:MF_00269};
DE Short=Prx {ECO:0000255|HAMAP-Rule:MF_00269};
DE AltName: Full=Scavengase p20 {ECO:0000303|PubMed:9141476};
DE AltName: Full=Thioredoxin peroxidase {ECO:0000255|HAMAP-Rule:MF_00269};
DE AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000255|HAMAP-Rule:MF_00269};
GN Name=tpx {ECO:0000255|HAMAP-Rule:MF_00269}; OrderedLocusNames=HI_0751;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP PROTEIN SEQUENCE OF 2-12, FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=9141476; DOI=10.1016/s0014-5793(97)00302-5;
RA Wan X.Y., Zhou Y., Yan Z.Y., Wang H.L., Hou Y.D., Jin D.Y.;
RT "Scavengase p20: a novel family of bacterial antioxidant enzymes.";
RL FEBS Lett. 407:32-36(1997).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), AND DISULFIDE BOND.
RA Kniewel R., Buglino J., Solorzano V., Wu J., Lima C.D.;
RT "Structure of a thiol peroxidase from Haemophilus influenzae Rd.";
RL Submitted (AUG-2003) to the PDB data bank.
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:0000255|HAMAP-Rule:MF_00269,
CC ECO:0000269|PubMed:9141476}.
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:0000255|HAMAP-
CC Rule:MF_00269, ECO:0000269|PubMed:9141476};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00269}.
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. In this atypical 2-Cys
CC peroxiredoxin, C(R) is present in the same subunit to form an
CC intramolecular disulfide. The disulfide is subsequently reduced by
CC thioredoxin. {ECO:0000255|HAMAP-Rule:MF_00269}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Tpx subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00269}.
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DR EMBL; L42023; AAC22410.1; -; Genomic_DNA.
DR PIR; G64090; G64090.
DR RefSeq; NP_438910.1; NC_000907.1.
DR RefSeq; WP_005693150.1; NC_000907.1.
DR PDB; 1Q98; X-ray; 1.90 A; A/B=1-165.
DR PDBsum; 1Q98; -.
DR AlphaFoldDB; Q57549; -.
DR SMR; Q57549; -.
DR STRING; 71421.HI_0751; -.
DR EnsemblBacteria; AAC22410; AAC22410; HI_0751.
DR KEGG; hin:HI_0751; -.
DR PATRIC; fig|71421.8.peg.788; -.
DR eggNOG; COG2077; Bacteria.
DR HOGENOM; CLU_042529_12_2_6; -.
DR OMA; ITQEPNY; -.
DR PhylomeDB; Q57549; -.
DR BioCyc; HINF71421:G1GJ1-789-MON; -.
DR EvolutionaryTrace; Q57549; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:UniProtKB-UniRule.
DR CDD; cd03014; PRX_Atyp2cys; 1.
DR HAMAP; MF_00269; Tpx; 1.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR InterPro; IPR002065; TPX.
DR InterPro; IPR018219; Tpx_CS.
DR Pfam; PF08534; Redoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
DR PROSITE; PS01265; TPX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antioxidant; Direct protein sequencing; Disulfide bond;
KW Oxidoreductase; Peroxidase; Redox-active center; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9141476"
FT CHAIN 2..165
FT /note="Thiol peroxidase"
FT /id="PRO_0000187880"
FT DOMAIN 17..165
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00269"
FT ACT_SITE 59
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00269"
FT DISULFID 59..93
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:1Q98"
FT DISULFID 59..93
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00269"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:1Q98"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:1Q98"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:1Q98"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:1Q98"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1Q98"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:1Q98"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:1Q98"
FT HELIX 61..72
FT /evidence="ECO:0007829|PDB:1Q98"
FT STRAND 76..84
FT /evidence="ECO:0007829|PDB:1Q98"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:1Q98"
FT TURN 93..97
FT /evidence="ECO:0007829|PDB:1Q98"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:1Q98"
FT HELIX 111..115
FT /evidence="ECO:0007829|PDB:1Q98"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:1Q98"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:1Q98"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:1Q98"
FT HELIX 157..162
FT /evidence="ECO:0007829|PDB:1Q98"
SQ SEQUENCE 165 AA; 17626 MW; 221DA969C76106CB CRC64;
MTVTLAGNPI EVGGHFPQVG EIVENFILVG NDLADVALND FASKRKVLNI FPSIDTGVCA
TSVRKFNQQA AKLSNTIVLC ISADLPFAQA RFCGAEGIEN AKTVSTFRNH ALHSQLGVDI
QTGPLAGLTS RAVIVLDEQN NVLHSQLVEE IKEEPNYEAA LAVLA
