Q9LDN9 (PER37_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peroxidase 37
Short name=Atperox P37
EC=1.11.1.7

Alternative name(s):
ATP38

Gene names

Name:	PER37
Synonyms:	P37
Ordered Locus Names:	At4g08770
ORF Names:	T32A17.80

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	346 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Removal of H2O2, oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic activity	2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O.
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per subunit By similarity. Binds 2 calcium ions per subunit By similarity.
Subcellular location	Secreted Probable. Vacuole Probable. Note: Carboxy-terminal extension appears to target the protein to vacuoles.
Miscellaneous	There are 73 peroxidase genes in A.thaliana.
Sequence similarities	Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Secreted Vacuole
Domain	Signal
Ligand	Calcium Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
PTM	Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of growth Inferred from mutant phenotype. Source: TAIR
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell vacuole Inferred from direct assay. Source: TAIR
Molecular function	heme binding Inferred from electronic annotation. Source: InterPro peroxidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Chain	23 – 346	324	Peroxidase 37		PRO_0000023703
Sites
	Active site	64	1	Proton acceptor By similarity
	Metal binding	65	1	Calcium 1 By similarity
	Metal binding	68	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	70	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	72	1	Calcium 1 By similarity
	Metal binding	74	1	Calcium 1 By similarity
	Metal binding	192	1	Iron (heme axial ligand) By similarity
	Metal binding	193	1	Calcium 2 By similarity
	Metal binding	244	1	Calcium 2 By similarity
	Metal binding	247	1	Calcium 2 By similarity
	Metal binding	252	1	Calcium 2 By similarity
	Binding site	161	1	Substrate; via carbonyl oxygen By similarity
	Site	60	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	23	1	Pyrrolidone carboxylic acid By similarity
	Glycosylation	79	1	N-linked (GlcNAc...) Potential
	Glycosylation	208	1	N-linked (GlcNAc...) Potential
	Glycosylation	236	1	N-linked (GlcNAc...) Potential
	Disulfide bond	33 ↔ 113		By similarity
	Disulfide bond	66 ↔ 71		By similarity
	Disulfide bond	119 ↔ 323		By similarity
	Disulfide bond	199 ↔ 231		By similarity
Experimental info
	Sequence conflict	28	1	F → L in AAM97030. Ref.4
	Sequence conflict	28	1	F → L in AAN15499. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9LDN9 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 744A4B8B618E15EE	FASTA	346	38,203
	10 20 30 40 50 60 MHSSLIKLGF LLLLIQVSLS HAQLSPSFYD KTCPQVFDIA TTTIVNALRS DPRIAASILR 70 80 90 100 110 120 LHFHDCFVNG CDASILLDNT TSFRTEKDAF GNANSARGFD VIDKMKAAVE KACPKTVSCA 130 140 150 160 170 180 DLLAIAAQES VVLAGGPSWR VPNGRRDSLR GFMDLANDNL PAPFFTLNQL KDRFKNVGLD 190 200 210 220 230 240 RASDLVALSG GHTFGKNQCQ FIMDRLYNFS NTGLPDPTLD KSYLSTLRKQ CPRNGNQSVL 250 260 270 280 290 300 VDFDLRTPTL FDNKYYVNLK ENKGLIQSDQ ELFSSPDASD TLPLVREYAD GQGKFFDAFA 310 320 330 340 KAMIRMSSLS PLTGKQGEIR LNCRVVNSKS KIMDVVEDAL EFASSM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural diversity and transcription of class III peroxidases from Arabidopsis thaliana." Welinder K.G., Justesen A.F., Kjaersgaard I.V.H., Jensen R.B., Rasmussen S.K., Jespersen H.M., Duroux L. Eur. J. Biochem. 269:6063-6081(2002) [PubMed: 12473102] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia. Tissue: Root.
[2]	"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.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"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.
[5]	"Analysis and expression of the class III peroxidase large gene family in Arabidopsis thaliana." Tognolli M., Penel C., Greppin H., Simon P. Gene 288:129-138(2002) [PubMed: 12034502] [Abstract] Cited for: GENE FAMILY ORGANIZATION, NOMENCLATURE. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF452387 mRNA. Translation: AAL40851.1. AL161512 Genomic DNA. Translation: CAB78002.1. AL161813 Genomic DNA. Translation: CAB82113.1. CP002687 Genomic DNA. Translation: AEE82676.1. AY136364 mRNA. Translation: AAM97030.1. BT000180 mRNA. Translation: AAN15499.1.
IPI	IPI00545315.
PIR	B85088.
RefSeq	NP_192617.1. NM_116947.2.
UniGene	At.4181. At.54214.
3D structure databases
ProteinModelPortal	Q9LDN9.
SMR	Q9LDN9. Positions 23-327.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9LDN9.
Protein family/group databases
PeroxiBase	203. AtPrx37.
Proteomic databases
PRIDE	Q9LDN9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G08770.1; AT4G08770.1; AT4G08770.
GeneID	826447.
GenomeReviews	Gene locus AT4G08770 in contig CT486007_GR.
KEGG	ath:AT4G08770.
NMPDR	fig|3702.1.peg.18530.
Organism-specific databases
GeneFarm	1864. 61.
TAIR	At4g08770.
Phylogenomic databases
GeneTree	EPGT00070000028241.
HOGENOM	HBG597790.
InParanoid	Q9LDN9.
OMA	FAKAMIR.
PhylomeDB	Q9LDN9.
ProtClustDB	CLSN2683115.
Gene expression databases
ArrayExpress	Q9LDN9.
Genevestigator	Q9LDN9.
GermOnline	AT4G08770. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR010255. Haem_peroxidase. IPR002016. Haem_peroxidase_pln/fun/bac. IPR000823. Peroxidase_pln. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [Graphical view]
KO	K00430.
Pfam	PF00141. peroxidase. 1 hit. [Graphical view]
PRINTS	PR00458. PEROXIDASE. PR00461. PLPEROXIDASE.
SUPFAM	SSF48113. Peroxidase_super. 1 hit.
PROSITE	PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PER37_ARATH

Accession

Primary (citable) accession number: Q9LDN9
Secondary accession number(s): Q8L7B3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2002
Last sequence update:	October 1, 2000
Last modified:	December 14, 2011
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program