ID   TL29_SOLLC              Reviewed;         345 AA.
AC   Q9THX6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Thylakoid lumenal 29 kDa protein, chloroplastic;
DE            Short=TL29;
DE            EC=1.-.-.-;
DE   AltName: Full=LeAPx09;
DE   AltName: Full=P29;
DE   Flags: Precursor;
GN   Name=CLEB3J9;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX   PubMed=11034343; DOI=10.1016/s0014-5793(00)01890-1;
RA   Kieselbach T., Bystedt M., Hynds P., Robinson C., Schroeder W.P.;
RT   "A peroxidase homologue and novel plastocyanin located by proteomics to the
RT   Arabidopsis chloroplast thylakoid lumen.";
RL   FEBS Lett. 480:271-276(2000).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC       {ECO:0000269|PubMed:11034343}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. {ECO:0000305}.
CC   -!- CAUTION: Probably not an ascorbate peroxidase (APx), as it lacks the
CC       heme-binding site, the proton acceptor and the transition state
CC       stabilizer, which are conserved features of the ascorbate peroxidase.
CC       {ECO:0000305}.
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DR   EMBL; AJ251882; CAB64343.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9THX6; -.
DR   SMR; Q9THX6; -.
DR   STRING; 4081.Solyc04g074640.2.1; -.
DR   PeroxiBase; 3921; LeAPx09.
DR   PaxDb; Q9THX6; -.
DR   PRIDE; Q9THX6; -.
DR   eggNOG; ENOG502QR5T; Eukaryota.
DR   InParanoid; Q9THX6; -.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; Q9THX6; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR   GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR   GO; GO:0000302; P:response to reactive oxygen species; IBA:GO_Central.
DR   InterPro; IPR044831; Ccp1-like.
DR   InterPro; IPR002016; Haem_peroxidase.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR002207; Peroxidase_I.
DR   PANTHER; PTHR31356; PTHR31356; 1.
DR   Pfam; PF00141; peroxidase; 1.
DR   PRINTS; PR00459; ASPEROXIDASE.
DR   SUPFAM; SSF48113; SSF48113; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Oxidoreductase; Plastid; Reference proteome; Thylakoid;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   TRANSIT         ?..78
FT                   /note="Thylakoid"
FT                   /evidence="ECO:0000250"
FT   CHAIN           79..345
FT                   /note="Thylakoid lumenal 29 kDa protein, chloroplastic"
FT                   /id="PRO_0000023636"
SQ   SEQUENCE   345 AA;  37750 MW;  681CAEBFDDBEB41B CRC64;
     MVSFASTLPS LVSFIPSPSS ITNASRNPPQ PGMICCKFRS ELNNEDRFHR RDILQSVGAA
     VGMDLIARSS AFIEVANAAD LIQRRQRSDF QSKIKLTLYD AIKANPDIIP SLLTLALNDA
     ITYDKATKTG GPNGSIRFSS EISRPENKGL DAALNLLEES KKVIDLDSKG GPISYADLIQ
     FAAQSAVKST FIASAISKCG GNVEKGTLLY SAYGSNGQWG QFDRIFGRSD AQEPDPEGRV
     PQWDKASVQE MKDKFKAVGL GPRQLAVMSS FLGPDQAATE ALLASDPEVL PWIQKYQRSR
     ETVSRTDYEV DLITTVTKLS SLGQVINYEA YTYPPRKIDV TKLKL