ID   APXT_ARATH              Reviewed;         426 AA.
AC   Q42593; Q9CAQ6;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   16-JUN-2009, entry version 56.
DE   RecName: Full=L-ascorbate peroxidase T, chloroplastic;
DE            EC=1.11.1.11;
DE   AltName: Full=Thylakoid-bound ascorbate peroxidase;
DE            Short=tAPX;
DE            Short=AtAPx06;
DE   Flags: Precursor;
GN   Name=APXT; OrderedLocusNames=At1g77490; ORFNames=T5M16.8;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=97419079; PubMed=9291097;
RA   Jespersen H.M., Kjaersgaard I.V.H., Oestergaard L., Welinder K.G.;
RT   "From sequence analysis of three novel ascorbate peroxidases from
RT   Arabidopsis thaliana to structure, function and evolution of seven
RT   types of ascorbate peroxidase.";
RL   Biochem. J. 326:305-310(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16034597; DOI=10.1007/s00425-005-0028-8;
RA   Panchuk I.I., Zentgraf U., Volkov R.A.;
RT   "Expression of the Apx gene family during leaf senescence of
RT   Arabidopsis thaliana.";
RL   Planta 222:926-932(2005).
CC   -!- FUNCTION: Plays a key role in hydrogen peroxide removal (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: L-ascorbate + H(2)O(2) = dehydroascorbate + 2
CC       H(2)O.
CC   -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per
CC       subunit.
CC   -!- COFACTOR: Binds 1 potassium or calcium ion per subunit (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane;
CC       Single-pass membrane protein (Potential).
CC   -!- DEVELOPMENTAL STAGE: Down-regulated during leaf senescence.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase
CC       subfamily.
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DR   EMBL; X98926; CAA67426.1; -; mRNA.
DR   EMBL; AC010704; AAG51660.1; -; Genomic_DNA.
DR   EMBL; AK229693; BAF01533.1; -; mRNA.
DR   EMBL; AY085554; AAM62777.1; -; mRNA.
DR   IPI; IPI00542810; -.
DR   PIR; C96804; C96804.
DR   RefSeq; NP_177873.1; -.
DR   UniGene; At.25463; -.
DR   HSSP; Q8LNY5; 1IYN.
DR   SMR; Q42593; 79-352.
DR   PRIDE; Q42593; -.
DR   GeneID; 844085; -.
DR   GenomeReviews; CT485782_GR; AT1G77490.
DR   KEGG; ath:AT1G77490; -.
DR   NMPDR; fig|3702.1.peg.7290; -.
DR   GeneFarm; 1953; 146.
DR   TAIR; At1g77490; -.
DR   BRENDA; 1.11.1.11; 302.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0016688; F:L-ascorbate peroxidase activity; IEA:EC.
DR   GO; GO:0030955; F:potassium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002207; Asc_perxdse.
DR   InterPro; IPR002016; Haem_peroxidase_pln/fun/bac.
DR   InterPro; IPR019794; Peroxidases_AS.
DR   InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR   Pfam; PF00141; peroxidase; 1.
DR   PRINTS; PR00459; ASPEROXIDASE.
DR   PRINTS; PR00458; PEROXIDASE.
DR   PROSITE; PS00435; PEROXIDASE_1; 1.
DR   PROSITE; PS00436; PEROXIDASE_2; FALSE_NEG.
DR   PROSITE; PS50873; PEROXIDASE_4; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Chloroplast; Complete proteome; Heme; Hydrogen peroxide;
KW   Iron; Membrane; Metal-binding; Oxidoreductase; Peroxidase; Plastid;
KW   Potassium; Thylakoid; Transit peptide; Transmembrane.
FT   TRANSIT       1      ?       Chloroplast (Potential).
FT   TRANSIT       ?     78       Thylakoid (Potential).
FT   CHAIN        79    426       L-ascorbate peroxidase T, chloroplastic.
FT                                /FTId=PRO_0000261327.
FT   TRANSMEM    397    417       Potential.
FT   ACT_SITE    112    112       Proton acceptor (By similarity).
FT   METAL       241    241       Iron (heme axial ligand) (By similarity).
FT   METAL       242    242       Potassium or calcium (By similarity).
FT   METAL       274    274       Potassium or calcium (By similarity).
FT   METAL       281    281       Potassium or calcium (By similarity).
FT   SITE        108    108       Transition state stabilizer (By
FT                                similarity).
FT   CONFLICT     73     73       M -> K (in Ref. 1; CAA67426).
SQ   SEQUENCE   426 AA;  46092 MW;  9205E8E77B73BBAC CRC64;
     MSVSLSAASH LLCSSTRVSL SPAVTSSSSS PVVALSSSTS PHSLGSVASS SLFPHSSFVL
     QKKHPINGTS TRMISPKCAA SDAAQLISAK EDIKVLLRTK FCHPILVRLG WHDAGTYNKN
     IEEWPLRGGA NGSLRFEAEL KHAANAGLLN ALKLIQPLKD KYPNISYADL FQLASATAIE
     EAGGPDIPMK YGRVDVVAPE QCPEEGRLPD AGPPSPADHL RDVFYRMGLD DKEIVALSGA
     HTLGRARPDR SGWGKPETKY TKTGPGEAGG QSWTVKWLKF DNSYFKDIKE KRDDDLLVLP
     TDAALFEDPS FKNYAEKYAE DVAAFFKDYA EAHAKLSNLG AKFDPPEGIV IENVPEKFVA
     AKYSTGKKEL SDSMKKKIRA EYEAIGGSPD KPLPTNYFLN IIIAIGVLVL LSTLFGGNNN
     SDFSGF
//