APXS_ARATH
ID APXS_ARATH Reviewed; 372 AA.
AC Q42592; Q9STM9;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=L-ascorbate peroxidase S, chloroplastic/mitochondrial;
DE EC=1.11.1.11;
DE AltName: Full=Stromal ascorbate peroxidase;
DE Short=AtAPx05;
DE Short=sAPX;
DE Flags: Precursor;
GN Name=APXS; OrderedLocusNames=At4g08390; ORFNames=T28D5.80;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=12954611; DOI=10.1074/jbc.m307525200;
RA Chew O., Whelan J., Millar A.H.;
RT "Molecular definition of the ascorbate-glutathione cycle in Arabidopsis
RT mitochondria reveals dual targeting of antioxidant defenses in plants.";
RL J. Biol. Chem. 278:46869-46877(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP ASN-91.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
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: Mitochondrion {ECO:0000269|PubMed:12954611,
CC ECO:0000305|PubMed:25732537}. Plastid, chloroplast stroma
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q42592-1; Sequence=Displayed;
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; X98925; CAA67425.1; -; mRNA.
DR EMBL; AL109819; CAB52561.1; -; Genomic_DNA.
DR EMBL; AL161511; CAB77964.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82634.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82635.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67521.1; -; Genomic_DNA.
DR EMBL; AY056319; AAL07168.1; -; mRNA.
DR EMBL; AY114065; AAM45113.1; -; mRNA.
DR PIR; T14193; T14193.
DR RefSeq; NP_001319883.1; NM_001340582.1. [Q42592-1]
DR RefSeq; NP_192579.1; NM_116908.3. [Q42592-1]
DR RefSeq; NP_974520.1; NM_202791.3. [Q42592-1]
DR AlphaFoldDB; Q42592; -.
DR SMR; Q42592; -.
DR STRING; 3702.AT4G08390.1; -.
DR PeroxiBase; 1886; AtAPx05.
DR iPTMnet; Q42592; -.
DR PaxDb; Q42592; -.
DR PRIDE; Q42592; -.
DR EnsemblPlants; AT4G08390.1; AT4G08390.1; AT4G08390. [Q42592-1]
DR EnsemblPlants; AT4G08390.2; AT4G08390.2; AT4G08390. [Q42592-1]
DR EnsemblPlants; AT4G08390.5; AT4G08390.5; AT4G08390. [Q42592-1]
DR GeneID; 826396; -.
DR Gramene; AT4G08390.1; AT4G08390.1; AT4G08390. [Q42592-1]
DR Gramene; AT4G08390.2; AT4G08390.2; AT4G08390. [Q42592-1]
DR Gramene; AT4G08390.5; AT4G08390.5; AT4G08390. [Q42592-1]
DR KEGG; ath:AT4G08390; -.
DR Araport; AT4G08390; -.
DR TAIR; locus:2137435; AT4G08390.
DR eggNOG; ENOG502QS7Q; Eukaryota.
DR InParanoid; Q42592; -.
DR OrthoDB; 1228462at2759; -.
DR PhylomeDB; Q42592; -.
DR BioCyc; ARA:AT4G08390-MON; -.
DR BRENDA; 1.11.1.11; 399.
DR PRO; PR:Q42592; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q42592; baseline and differential.
DR Genevisible; Q42592; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA: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: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 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 1: Evidence at protein level;
KW Alternative splicing; Calcium; Chloroplast; Heme; Hydrogen peroxide; Iron;
KW Metal-binding; Mitochondrion; Oxidoreductase; Peroxidase; Plastid;
KW Potassium; Reference proteome; Transit peptide.
FT TRANSIT 1..91
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 92..372
FT /note="L-ascorbate peroxidase S,
FT chloroplastic/mitochondrial"
FT /id="PRO_0000261326"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 133
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 262
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 263
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT SITE 129
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CONFLICT 11
FT /note="G -> V (in Ref. 1; CAA67425)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="S -> P (in Ref. 1; CAA67425)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="Y -> C (in Ref. 1; CAA67425)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="V -> I (in Ref. 1; CAA67425)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 372 AA; 40407 MW; A5D94B9A20720B87 CRC64;
MAERVSLTLN GTLLSPPPTT TTTTMSSSLR STTAASLLLR SSSSSSRSTL TLSASSSLSF
VRSLVSSPRL SSSSSLSQKK YRIASVNRSF NSTTAATKSS SSDPDQLKNA REDIKELLST
KFCHPILVRL GWHDAGTYNK NIKEWPQRGG ANGSLRFDIE LKHAANAGLV NALNLIKDIK
EKYSGISYAD LFQLASATAI EEAGGPKIPM KYGRVDASGP EDCPEEGRLP DAGPPSPATH
LREVFYRMGL DDKDIVALSG AHTLGRSRPE RSGWGKPETK YTKEGPGAPG GQSWTPEWLK
FDNSYFKEIK EKRDEDLLVL PTDAAIFEDS SFKVYAEKYA ADQDAFFKDY AVAHAKLSNL
GAEFNPPEGI VI
