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Protein

Glutathione peroxidase 1, mitochondrial

Gene

GPX

Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May constitute a glutathione peroxidase-like protective system against oxidative stresses. Hydrogen peroxide, tert-butyl hydroperoxide and cumene, but not phosphatidylcholine hydroperoxide, can act as acceptors.1 Publication

Catalytic activityi

2 glutathione + H2O2 = glutathione disulfide + 2 H2O.1 Publication

GO - Molecular functioni

  • glutathione peroxidase activity Source: UniProtKB

GO - Biological processi

  • cellular oxidant detoxification Source: GOC
  • response to oxidative stress Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Ligandi

Selenium

Protein family/group databases

PeroxiBasei2590. CreGPx02.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione peroxidase 1, mitochondrial1 Publication (EC:1.11.1.9)
Short name:
CrGPx11 Publication
Gene namesi
Name:GPXImported
Synonyms:PHGPX11 Publication
ORF Names:CHLREDRAFT_206090
OrganismiChlamydomonas reinhardtii (Chlamydomonas smithii)
Taxonomic identifieri3055 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas
Proteomesi
  • UP000006906 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2727MitochondrionAdd
BLAST
Chaini28 – 201174Glutathione peroxidase 1, mitochondrialSequence analysisPRO_0000013089Add
BLAST

Proteomic databases

PaxDbiP83564.
PRIDEiP83564.

Expressioni

Inductioni

By selenium, particularly under autotrophic conditions.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi3055.EDP06633.

Structurei

3D structure databases

ProteinModelPortaliP83564.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glutathione peroxidase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1651. Eukaryota.
COG0386. LUCA.
InParanoidiP83564.
KOiK00432.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000889. Glutathione_peroxidase.
IPR029759. GPX_AS.
IPR029760. GPX_CS.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR11592. PTHR11592. 1 hit.
PfamiPF00255. GSHPx. 1 hit.
[Graphical view]
PIRSFiPIRSF000303. Glutathion_perox. 1 hit.
PRINTSiPR01011. GLUTPROXDASE.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P83564-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLTRKNVAV RPARAARRDV RAMSLLGNLF GGGSKPTSST SNFHQLSALD
60 70 80 90 100
IDKKNVDFKS LNNRVVLVVN VASKUGLTAA NYKEFATLLG KYPATDLTIV
110 120 130 140 150
AFPCNQFGGQ EPGTNAEIKA FASARGFSGA GALLMDKVDV NGANASPVYN
160 170 180 190 200
FLKVAAGDTS DIGWNFGKFL VRPDGTVFGR YAPTTGPLSL EKYIVELINS

R
Length:201
Mass (Da):21,499
Last modified:February 26, 2008 - v2
Checksum:i1030F45EBA62C219
GO

Mass spectrometryi

Molecular mass is 18496 Da from positions 28 - 201. Determined by MALDI. 1 Publication
Molecular mass is 18571 Da from positions 28 - 201. Determined by ESI. 1 Publication

Non-standard residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-standard residuei75 – 751Selenocysteine2 Publications

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY051144 mRNA. Translation: AAL14348.1.
DS496114 Genomic DNA. Translation: EDP06633.1.
RefSeqiXP_001701658.1. XM_001701606.1.
UniGeneiCre.4579.

Genome annotation databases

EnsemblPlantsiEDP06633; EDP06633; CHLREDRAFT_206090.
GeneIDi5727250.
GrameneiEDP06633; EDP06633; CHLREDRAFT_206090.
KEGGicre:CHLREDRAFT_206090.

Keywords - Coding sequence diversityi

Selenocysteine

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY051144 mRNA. Translation: AAL14348.1.
DS496114 Genomic DNA. Translation: EDP06633.1.
RefSeqiXP_001701658.1. XM_001701606.1.
UniGeneiCre.4579.

3D structure databases

ProteinModelPortaliP83564.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3055.EDP06633.

Protein family/group databases

PeroxiBasei2590. CreGPx02.

Proteomic databases

PaxDbiP83564.
PRIDEiP83564.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiEDP06633; EDP06633; CHLREDRAFT_206090.
GeneIDi5727250.
GrameneiEDP06633; EDP06633; CHLREDRAFT_206090.
KEGGicre:CHLREDRAFT_206090.

Phylogenomic databases

eggNOGiKOG1651. Eukaryota.
COG0386. LUCA.
InParanoidiP83564.
KOiK00432.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000889. Glutathione_peroxidase.
IPR029759. GPX_AS.
IPR029760. GPX_CS.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR11592. PTHR11592. 1 hit.
PfamiPF00255. GSHPx. 1 hit.
[Graphical view]
PIRSFiPIRSF000303. Glutathion_perox. 1 hit.
PRINTSiPR01011. GLUTPROXDASE.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A selenoprotein in the plant kingdom. Mass spectrometry confirms that an opal codon (UGA) encodes selenocysteine in Chlamydomonas reinhardtii glutathione peroxidase."
    Fu L.-H., Wang X.-F., Eyal Y., She Y.-M., Donald L.J., Standing K.G., Ben-Hayyim G.
    J. Biol. Chem. 277:25983-25991(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, INDUCTION, SELENOCYSTEINE AT SEC-75, MASS SPECTROMETRY.
    Strain: 2137.
  2. "The Chlamydomonas genome reveals the evolution of key animal and plant functions."
    Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J., Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L., Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H., Kapitonov V.V., Ren Q., Ferris P.
    , Lindquist E., Shapiro H., Lucas S.M., Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L., Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H., Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M., Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A., Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L., Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C., Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J., Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L., Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L., Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C., Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J., Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P., Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R., Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P., Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y., Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L., Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.
    Science 318:245-250(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CC-503.
  3. "Selenoproteins and selenocysteine insertion system in the model plant cell system, Chlamydomonas reinhardtii."
    Novoselov S.V., Rao M., Onoshko N.V., Zhi H., Kryukov G.V., Xiang Y., Weeks D.P., Hatfield D.L., Gladyshev V.N.
    EMBO J. 21:3681-3693(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SELENOCYSTEINE AT SEC-75.

Entry informationi

Entry nameiGPX1_CHLRE
AccessioniPrimary (citable) accession number: P83564
Secondary accession number(s): A8IAD7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: February 26, 2008
Last modified: February 17, 2016
This is version 71 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.