Ascorbate peroxidase - Glycine max (Soybean)

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Q43758 (Q43758_SOYBN) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 87. History...

Clusters with 100%, 90%, 50% identity |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Submitted name:
Ascorbate peroxidase EMBL AAA61779.1
EC=1.11.1.11 EMBL AAA61779.1

Submitted name:
Cytosolic ascorbate peroxidase 1 EMBL BAC92739.1
EC=1.11.1.11 EMBL BAC92739.1
Submitted name:
Uncharacterized protein EnsemblPlants GLYMA11G15680.5

Gene names

Name:

apx1 EMBL BAC92739.1

Organism

Glycine max (Soybean) (Glycine hispida) [Reference proteome] EMBL AAA61779.1

Taxonomic identifier

3847 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Phaseoleae › Glycine

Protein attributes

Sequence length	250 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the peroxidase family. RuleBase RU004241

Ontologies

Keywords
Ligand	Heme PDB 2VCF PDB 2XI6 PDB 2XJ6 PDB 2CL4 PDB 2VCN PDB 1V0H PDB 1OAG PDB 2VNZ PDB 1OAF PDB 2GHE PDB 2XIF PDB 2VCS PDB 2GHC PDB 2GHD PDB 2VO2 PDB 2XIH PDB 2GHH PDB 2GHK PDB 2GGN PDB 2VNX Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase EMBL AAA61779.1
Technical term	3D-structure PDB 2VCF PDB 2XI6 PDB 2XJ6 PDB 2CL4 PDB 2VCN PDB 1V0H PDB 1OAG PDB 2VNZ PDB 1OAF PDB 2GHE PDB 2XIF PDB 2VCS PDB 2GHC PDB 2WD4 PDB 2GHD PDB 2VO2 PDB 2XIH PDB 2GHH PDB 2GHK PDB 2GGN PDB 2VNX PDB 3ZCY PDB 3ZCH PDB 3ZCG PDB 2Y6B PDB 2Y6A Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	response to oxidative stress Inferred from electronic annotation. Source: InterPro
Molecular_function	L-ascorbate peroxidase activity Inferred from electronic annotation. Source: EC heme binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Regions

Region

34 – 35

Ascorbic acid binding PDB 1OAF

Sites

Metal binding

Iron (heme axial ligand); via tele nitrogen

Metal binding

163

Iron (heme axial ligand); via tele nitrogen PDB 2VCF PDB 2XI6 PDB 2XJ6 PDB 2CL4 PDB 2VCN PDB 1V0H PDB 1OAG PDB 2VNZ PDB 1OAF PDB 2GHE PDB 2XIF PDB 2VCS PDB 2GHC PDB 2GHD PDB 2VO2 PDB 2XIH PDB 2GHH PDB 2GHK PDB 2GGN PDB 2VNX

Binding site

Ascorbic acid PDB 1OAF

Binding site

172

Ascorbic acid PDB 1OAF

Sequences

Sequence

Length

Mass (Da)

Tools

Q43758 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: CEEB996CCCBBF201
Show »

FASTA

250

27,052

        10         20         30         40         50         60 
MGKSYPTVSA DYQKAVEKAK KKLRGFIAEK RCAPLMLRLA WHSAGTFDKG TKTGGPFGTI 

        70         80         90        100        110        120 
KHPAELAHSA NNGLDIAVRL LEPLKAEFPI LSYADFYQLA GVVAVEVTGG PEVPFHPGRE 

       130        140        150        160        170        180 
DKPEPPPEGR LPDATKGSDH LRDVFGKAMG LTDQDIVALS GGHTIGAAHK ERSGFEGPWT 

       190        200        210        220        230        240 
SNPLIFDNSY FTELLSGEKE GLLQLPSDKA LLSDPVFRPL VDKYAADEDA FFADYAEAHQ 

       250 
KLSELGFADA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Ascorbate peroxidase from soybean root nodules." Chatfield M., Dalton D.A. Plant Physiol. 103:661-662(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Tissue: Root nodule EMBL AAA61779.1.
[2]	"Deficiency of a cytosolic ascorbate peroxidase associated with chilling tolerance in soybean." Funatsuki H. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[3]	"Crystal structure of the ascorbate peroxidase-ascorbate complex." Sharp K.H., Mewies M., Moody P.C., Raven E.L. Nat. Struct. Biol. 10:303-307(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 2-250 IN COMPLEX WITH ASCORBIC ACID AND HEME.
[4]	"Crystal structure of the ascorbate peroxidase-salicylhydroxamic acid complex." Sharp K.H., Moody P.C., Brown K.A., Raven E.L. Biochemistry 43:8644-8651(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) OF 2-250 IN COMPLEX WITH HEME.
[5]	"Interaction of ascorbate peroxidase with substrates: a mechanistic and structural analysis." Macdonald I.K., Badyal S.K., Ghamsari L., Moody P.C., Raven E.L. Biochemistry 45:7808-7817(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-250 IN COMPLEX WITH HEME.
[6]	"Conformational mobility in the active site of a heme peroxidase." Badyal S.K., Joyce M.G., Sharp K.H., Seward H.E., Mewies M., Basran J., Macdonald I.K., Moody P.C., Raven E.L. J. Biol. Chem. 281:24512-24520(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 2-250 IN COMPLEX WITH HEME.
[7]	"Iron oxidation state modulates active site structure in a heme peroxidase." Badyal S.K., Metcalfe C.L., Basran J., Efimov I., Moody P.C., Raven E.L. Biochemistry 47:4403-4409(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 2-250 IN COMPLEX WITH HEME.
[8]	"The tuberculosis prodrug isoniazid bound to activating peroxidases." Metcalfe C., Macdonald I.K., Murphy E.J., Brown K.A., Raven E.L., Moody P.C. J. Biol. Chem. 283:6193-6200(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 2-250 IN COMPLEX WITH HEME.
[9]	"Evidence for heme oxygenase activity in a heme peroxidase." Badyal S.K., Eaton G., Mistry S., Pipirou Z., Basran J., Metcalfe C.L., Gumiero A., Handa S., Moody P.C., Raven E.L. Biochemistry 48:4738-4746(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 2-250.
[10]	"Genome sequence of the palaeopolyploid soybean." Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D., Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D. Jackson S.A. Nature 463:178-183(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Williams 82 EnsemblPlants GLYMA11G15680.5.
[11]	"Proton delivery to ferryl heme in a heme peroxidase: enzymatic use of the Grotthuss mechanism." Efimov I., Badyal S.K., Metcalfe C.L., Macdonald I., Gumiero A., Raven E.L., Moody P.C. J. Am. Chem. Soc. 133:15376-15383(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-250.
[12]	"Nature of the ferryl heme in compounds I and II." Gumiero A., Metcalfe C.L., Pearson A.R., Raven E.L., Moody P.C. J. Biol. Chem. 286:1260-1268(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 2-250 IN COMPLEX WITH HEME.
[13]	EnsemblPlants Submitted (NOV-2012) to UniProtKB Cited for: IDENTIFICATION. Strain: Williams 82 EnsemblPlants GLYMA11G15680.5.
[14]	"Probing the conformational mobility of the active site of a heme peroxidase." Guimero A., Badyal S.K., Leeks T., Moody P.C., Raven E.L. Dalton Trans 42:3170-3175(2013) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) OF 2-250.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB082930 Genomic DNA. No translation available.
L10292 mRNA. Translation: AAA61779.1.
AB082931 mRNA. Translation: BAC92739.1.

RefSeq

NP_001237785.1. NM_001250856.1.

UniGene

Gma.1246.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OAF	X-ray	1.40	A	2-250	[»]
1OAG	X-ray	1.75	A	2-250	[»]
1V0H	X-ray	1.46	X	2-250	[»]
2CL4	X-ray	1.80	X	2-250	[»]
2GGN	X-ray	1.35	X	2-250	[»]
2GHC	X-ray	1.25	X	2-250	[»]
2GHD	X-ray	1.40	X	2-250	[»]
2GHE	X-ray	1.75	X	2-250	[»]
2GHH	X-ray	2.01	X	2-250	[»]
2GHK	X-ray	2.00	X	2-250	[»]
2VCF	X-ray	1.80	X	2-250	[»]
2VCN	X-ray	1.20	A	2-250	[»]
2VCS	X-ray	1.68	A	2-250	[»]
2VNX	X-ray	1.50	X	2-250	[»]
2VNZ	X-ray	1.30	X	2-250	[»]
2VO2	X-ray	1.90	X	2-250	[»]
2WD4	X-ray	1.40	A	2-250	[»]
2XI6	X-ray	1.65	A	2-250	[»]
2XIF	X-ray	1.65	A	2-250	[»]
2XIH	X-ray	1.65	A	2-250	[»]
2XJ6	X-ray	1.70	A	2-250	[»]
2Y6A	X-ray	2.00	A	2-250	[»]
2Y6B	X-ray	1.90	A	2-250	[»]
3ZCG	X-ray	1.49	A	2-250	[»]
3ZCH	X-ray	2.00	A	2-250	[»]
3ZCY	X-ray	2.00	A	2-250	[»]

SMR

Q43758. Positions 2-250.

ModBase

Search...

Protein family/group databases

PeroxiBase

1954. GmAPx01.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

GLYMA11G15680.5; GLYMA11G15680.5; GLYMA11G15680.

GeneID

553156.

KEGG

gmx:553156.

Phylogenomic databases

K00434.

Gene expression databases

Genevestigator

Q43758.

Family and domain databases

InterPro

IPR002207. Asc_peroxidase.
IPR010255. Haem_peroxidase.
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.

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...

Other

EvolutionaryTrace

Q43758.

Entry information

Entry name

Q43758_SOYBN

Accession

Primary (citable) accession number: Q43758

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1996
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information