Reviewed, UniProtKB/Swiss-Prot Q8GY91 (APX6_ARATH)

Names and origin

Protein names

Recommended name:
    Putative L-ascorbate peroxidase 6
      Short name=AtAPx08
    EC=1.11.1.11

Gene names

Name:	APX6
Ordered Locus Names:	At4g32320
ORF Names:	F10M6.50, F8B4.20

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	329 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Plays a key role in hydrogen peroxide removal By similarity.
Catalytic activity	L-ascorbate + H2O2 = dehydroascorbate + 2 H2O.
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per subunit.
Sequence similarities	Belongs to the peroxidase family. Ascorbate peroxidase subfamily.
Sequence caution	The sequence CAA16959.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAA22559.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB79949.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Traceable author statement. Source: TAIR
Molecular function	L-ascorbate peroxidase activity Inferred from electronic annotation. Source: EC heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 329	329	Putative L-ascorbate peroxidase 6		PRO_0000261325
Sites
	Active site	123	1	Proton acceptor By similarity
	Metal binding	244	1	Iron (heme axial ligand) By similarity
	Site	119	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8GY91-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: BC50726AB7B689DD	FASTA	329	36,240
	10 20 30 40 50 60 MTTTTASLVK TFLFRCDSFS SFKFKCKFES PAKTRLLSPA TEKHVVRSSR AWRIRCLSDD 70 80 90 100 110 120 PGSSHVFVAS RRKMVVLLST VQLLSHMLPQ NGNAAEIYPV MQNEIRKVVT KGKAAGVLRL 130 140 150 160 170 180 VFHDAGTFEL DDHSGGINGS IAYELERPEN IGLKKSLKVL AKAKVKVDEI QPVSWADMIS 190 200 210 220 230 240 VAGSEAVSIC GGPTIPVVLG RLDSAQPDPE GKLPPETLSA SGLKECFKRK GFSTQELVAL 250 260 270 280 290 300 SGAHTIGSKG FGDPTVFDNA YYKILLEKPW TSTSKMTSMV GLPSDHALVQ DDECLRWVKR 310 320 YAEDQDKFFE DFTNAYIKLV NSGAKWNML

References

[1]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"Functional annotation of a full-length Arabidopsis cDNA collection." Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K. Science 296:141-145(2002) [PubMed: 11910074] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL021811 Genomic DNA. Translation: CAA16959.1. Sequence problems. AL034567 Genomic DNA. Translation: CAA22559.1. Sequence problems. AL161581 Genomic DNA. Translation: CAB79949.1. Sequence problems. AK117784 mRNA. Translation: BAC42431.1. BT008349 mRNA. Translation: AAP37708.1.
IPI	IPI00526960.
PIR	T05342.
RefSeq	NP_194958.2.
UniGene	At.31673
3D structure databases
HSSP	HSSP built from PDB template 1APX based on UniProtKB P48534.
ModBase	Search...
Protein family/group databases
PeroxiBase	3952. AtAPx00.
Proteomic databases
PRIDE	Q8GY91.
Genome annotation databases
GeneID	829366.
GenomeReviews	Gene locus AT4G32320 in contig CT486007_GR.
KEGG	ath:AT4G32320.
NMPDR	fig|3702.1.peg.21252.
Organism-specific databases
GeneFarm	1981. 146.
TAIR	At4g32320.
Phylogenomic databases
OMA	DDECLRW.
Enzyme and pathway databases
BRENDA	1.11.1.11. 302.
Gene expression databases
Genevestigator	Q8GY91.
GermOnline	AT4G32320. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR002207. Asc_perxdse. IPR002016. Haem_peroxidase_pln/fun/bac. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [Graphical view]
Pfam	PF00141. peroxidase. 1 hit. [Graphical view]
PRINTS	PR00459. ASPEROXIDASE. PR00458. PEROXIDASE.
PROSITE	PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

APX6_ARATH

Accession

Primary (citable) accession number: Q8GY91
Secondary accession number(s): O49360

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	March 1, 2003
Last modified:	November 3, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)