APXT_ARATH
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 03-AUG-2022, entry version 136.
DE RecName: Full=L-ascorbate peroxidase T, chloroplastic;
DE EC=1.11.1.11;
DE AltName: Full=Thylakoid-bound ascorbate peroxidase;
DE Short=AtAPx06;
DE Short=tAPX;
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=9291097; DOI=10.1042/bj3260305;
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 types of
RT ascorbate peroxidase.";
RL Biochem. J. 326:305-310(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., 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., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
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., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 Arabidopsis
RT thaliana.";
RL Planta 222:926-932(2005).
CC -!- FUNCTION: Plays a key role in hydrogen peroxide removal. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O2 + L-ascorbate = 2 H2O + L-dehydroascorbate;
CC Xref=Rhea:RHEA:22996, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:58539; EC=1.11.1.11;
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Down-regulated during leaf senescence.
CC {ECO:0000269|PubMed:16034597}.
CC -!- MISCELLANEOUS: Binds one cation per subunit; probably K(+), but might
CC also be Ca(2+). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase
CC subfamily. {ECO:0000305}.
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DR EMBL; X98926; CAA67426.1; -; mRNA.
DR EMBL; AC010704; AAG51660.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35985.1; -; Genomic_DNA.
DR EMBL; AK229693; BAF01533.1; -; mRNA.
DR EMBL; AY085554; AAM62777.1; -; mRNA.
DR PIR; C96804; C96804.
DR RefSeq; NP_177873.1; NM_106398.3.
DR AlphaFoldDB; Q42593; -.
DR SMR; Q42593; -.
DR STRING; 3702.AT1G77490.1; -.
DR PeroxiBase; 1889; AtAPx06.
DR iPTMnet; Q42593; -.
DR PaxDb; Q42593; -.
DR PRIDE; Q42593; -.
DR EnsemblPlants; AT1G77490.1; AT1G77490.1; AT1G77490.
DR GeneID; 844085; -.
DR Gramene; AT1G77490.1; AT1G77490.1; AT1G77490.
DR KEGG; ath:AT1G77490; -.
DR Araport; AT1G77490; -.
DR TAIR; locus:2204735; AT1G77490.
DR eggNOG; ENOG502QS7Q; Eukaryota.
DR HOGENOM; CLU_036959_2_0_1; -.
DR InParanoid; Q42593; -.
DR OrthoDB; 1228462at2759; -.
DR PhylomeDB; Q42593; -.
DR BioCyc; ARA:AT1G77490-MON; -.
DR BRENDA; 1.11.1.11; 399.
DR PRO; PR:Q42593; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q42593; baseline and differential.
DR Genevisible; Q42593; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0016688; F:L-ascorbate peroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0010019; P:chloroplast-nucleus signaling pathway; IMP:TAIR.
DR GO; GO:0009631; P:cold acclimation; IMP:TAIR.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:0071588; P:hydrogen peroxide mediated signaling pathway; IMP:TAIR.
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 InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR PANTHER; PTHR31356; PTHR31356; 1.
DR Pfam; PF00141; peroxidase; 1.
DR PRINTS; PR00459; ASPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 2: Evidence at transcript level;
KW Calcium; Chloroplast; Heme; Hydrogen peroxide; Iron; Membrane;
KW Metal-binding; Oxidoreductase; Peroxidase; Plastid; Potassium;
KW Reference proteome; Thylakoid; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT ?..78
FT /note="Thylakoid"
FT /evidence="ECO:0000255"
FT CHAIN 79..426
FT /note="L-ascorbate peroxidase T, chloroplastic"
FT /id="PRO_0000261327"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 245..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 112
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 241
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 242
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT SITE 108
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CONFLICT 73
FT /note="M -> K (in Ref. 1; CAA67426)"
FT /evidence="ECO:0000305"
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
