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Protein
Submitted name:

APX protein

Gene

APX

Organism
Leishmania major
Status
Unreviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi69 – 691CalciumCombined sources
Metal bindingi69 – 691MagnesiumCombined sources
Metal bindingi72 – 721CalciumCombined sources
Metal bindingi72 – 721MagnesiumCombined sources
Metal bindingi81 – 811Calcium; via carbonyl oxygenCombined sources
Metal bindingi81 – 811Magnesium; via carbonyl oxygenCombined sources
Metal bindingi86 – 861CalciumCombined sources
Metal bindingi86 – 861MagnesiumCombined sources
Metal bindingi92 – 921CalciumCombined sources
Metal bindingi92 – 921MagnesiumCombined sources
Metal bindingi192 – 1921Iron (heme axial ligand); via tele nitrogenCombined sources

GO - Molecular functioni

  • cytochrome-c oxidase activity Source: GeneDB
  • heme binding Source: InterPro
  • iodide peroxidase activity Source: GeneDB
  • L-ascorbate oxidase activity Source: GeneDB
  • L-ascorbate peroxidase activity Source: GeneDB
  • metal ion binding Source: UniProtKB-KW
  • peroxidase activity Source: GeneDB

GO - Biological processi

  • calcium ion homeostasis Source: GeneDB
  • hydrogen ion transmembrane transport Source: GOC
  • hydrogen peroxide catabolic process Source: GeneDB
  • negative regulation of apoptotic process Source: GeneDB
  • reactive oxygen species metabolic process Source: GeneDB
  • response to drug Source: GeneDB
  • response to reactive oxygen species Source: GeneDB
  • stabilization of membrane potential Source: GeneDB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, PeroxidaseImported

Keywords - Ligandi

CalciumCombined sources, HemeCombined sources, Iron, MagnesiumCombined sources, Metal-binding

Enzyme and pathway databases

BRENDAi1.11.1.11. 2950.

Protein family/group databases

PeroxiBasei2334. LmAPx-CcP.

Names & Taxonomyi

Protein namesi
Submitted name:
APX proteinImported (EC:1.11.1.11Imported)
Gene namesi
Name:APXImported
ORF Names:LMJF_34_0070Imported
OrganismiLeishmania majorImported
Taxonomic identifieri5664 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania
ProteomesiUP000000542 Componenti: Chromosome 34

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: GeneDB
  • intrinsic component of mitochondrial inner membrane Source: GeneDB
Complete GO annotation...

Interactioni

Protein-protein interaction databases

DIPiDIP-60328N.
STRINGi5664.LmjF.34.0070.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3RIVX-ray1.76A/B35-303[»]
3RIWX-ray2.37A/B35-303[»]
4GEDX-ray1.84A35-301[»]
ProteinModelPortaliQ4Q3K2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peroxidase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000189824.
InParanoidiQ4Q3K2.
KOiK00434.
OMAiTICYEAS.

Family and domain databases

InterProiIPR002207. Asc_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
[Graphical view]
PfamiPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00459. ASPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q4Q3K2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGTSRRAKG LFTGIAVGTF VSGAMFVSCA SARVEEPPFD IRALRADIED
60 70 80 90 100
MISEKLELGP SLIRLAWHEA ASYDCFKKDG SPNSASMRFK PECLYAGNKG
110 120 130 140 150
LDIPRKALET LKKKYPQISY ADLWVLAAYV AIEYMGGPTI PFCWGRVDAK
160 170 180 190 200
DGSVCGPDGR LPDGSKTQSH VREVFRRLGF NDQETVALIG AHTCGECHIE
210 220 230 240 250
FSGYHGPWTH DKNGFDNSFF TQLLDEDWVL NPKVEQMQLM DRATTKLMML
260 270 280 290 300
PSDVCLLLDP SYRKYVELYA KDNDRFNKDF ANAFKKLTEL GTRNLHKAPA

SES
Length:303
Mass (Da):33,873
Last modified:July 19, 2005 - v1
Checksum:iB30DB35ACC26E8F0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FR796430 Genomic DNA. Translation: CAJ07706.1.
RefSeqiXP_001686096.1. XM_001686044.1.

Genome annotation databases

EnsemblProtistsiLmjF.34.0070:mRNA; LmjF.34.0070:pep; LmjF.34.0070.
GeneIDi5654759.
KEGGilma:LMJF_34_0070.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FR796430 Genomic DNA. Translation: CAJ07706.1.
RefSeqiXP_001686096.1. XM_001686044.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3RIVX-ray1.76A/B35-303[»]
3RIWX-ray2.37A/B35-303[»]
4GEDX-ray1.84A35-301[»]
ProteinModelPortaliQ4Q3K2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60328N.
STRINGi5664.LmjF.34.0070.

Protein family/group databases

PeroxiBasei2334. LmAPx-CcP.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiLmjF.34.0070:mRNA; LmjF.34.0070:pep; LmjF.34.0070.
GeneIDi5654759.
KEGGilma:LMJF_34_0070.

Phylogenomic databases

HOGENOMiHOG000189824.
InParanoidiQ4Q3K2.
KOiK00434.
OMAiTICYEAS.

Enzyme and pathway databases

BRENDAi1.11.1.11. 2950.

Family and domain databases

InterProiIPR002207. Asc_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
[Graphical view]
PfamiPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00459. ASPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome of the kinetoplastid parasite, Leishmania major."
    Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G., Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A., Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M., Bianchettin G.
    , Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E., Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., Davies R.M., De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N., Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A., Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S., Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M., Masuy D., Matthews K., Michaeli S., Mottram J.C., Muller-Auer S., Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M., Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E., Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C., Rutter S., Saunders D., Schafer M., Schein J., Schwartz D.C., Seeger K., Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V., Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J., Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D., Barrell B., Myler P.J.
    Science 309:436-442(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MHOM/IL/81/FriedlinImported.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FriedlinImported.
  3. "Crystal structure of Leishmania major peroxidase and characterization of the compound i tryptophan radical."
    Jasion V.S., Polanco J.A., Meharenna Y.T., Li H., Poulos T.L.
    J. Biol. Chem. 286:24608-24615(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 35-303 IN COMPLEX WITH CALCIUM AND HEME.
  4. "Crystal structure of the Leishmania major peroxidase-cytochrome c complex."
    Jasion V.S., Doukov T., Pineda S.H., Li H., Poulos T.L.
    Proc. Natl. Acad. Sci. U.S.A. 109:18390-18394(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 35-301 IN COMPLEX WITH HEME AND MAGNESIUM.

Entry informationi

Entry nameiQ4Q3K2_LEIMA
AccessioniPrimary (citable) accession number: Q4Q3K2
Entry historyi
Integrated into UniProtKB/TrEMBL: July 19, 2005
Last sequence update: July 19, 2005
Last modified: June 24, 2015
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.