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Protein

Peroxisomal (S)-2-hydroxy-acid oxidase GLO2

Gene

GLO2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

(S)-2-hydroxy acid + O2 = 2-oxo acid + H2O2.

Cofactori

FMNPROSITE-ProRule annotation

Pathway: photorespiration

This protein is involved in step 2 of the subpathway that synthesizes glycine from 2-phosphoglycolate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Peroxisomal (S)-2-hydroxy-acid oxidase GLO5 (GLO5), Peroxisomal (S)-2-hydroxy-acid oxidase GLO2 (GLO2), Peroxisomal (S)-2-hydroxy-acid oxidase GLO3 (GLO3), Peroxisomal (S)-2-hydroxy-acid oxidase GLO1 (GLO1), Peroxisomal (S)-2-hydroxy-acid oxidase GLO4 (GLO4)
  3. no protein annotated in this organism
This subpathway is part of the pathway photorespiration, which is itself part of Photosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes glycine from 2-phosphoglycolate, the pathway photorespiration and in Photosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei24 – 241SubstratePROSITE-ProRule annotation
Binding sitei106 – 1061FMNPROSITE-ProRule annotation
Binding sitei127 – 1271FMNPROSITE-ProRule annotation
Binding sitei129 – 1291SubstratePROSITE-ProRule annotation
Binding sitei155 – 1551FMNPROSITE-ProRule annotation
Binding sitei164 – 1641SubstratePROSITE-ProRule annotation
Binding sitei230 – 2301FMNPROSITE-ProRule annotation
Active sitei254 – 2541Proton acceptorPROSITE-ProRule annotation
Binding sitei257 – 2571SubstratePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi285 – 30925FMNPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolate pathway, Photorespiration

Keywords - Ligandi

Flavoprotein, FMN

Enzyme and pathway databases

BioCyciARA:AT3G14415-MONOMER.
ARA:GQT-740-MONOMER.
ARA:GQT-741-MONOMER.
ReactomeiREACT_278920. Glyoxylate metabolism.
UniPathwayiUPA00951; UER00912.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal (S)-2-hydroxy-acid oxidase GLO2 (EC:1.1.3.15)
Alternative name(s):
Glycolate oxidase 1
Short name:
AtGLO2
Short name:
GOX 1
Short chain alpha-hydroxy acid oxidase GLO2
Gene namesi
Name:GLO2
Synonyms:GOX1
Ordered Locus Names:At3g14415
ORF Names:MLN21.20
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G14415.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 367367Peroxisomal (S)-2-hydroxy-acid oxidase GLO2PRO_0000206323Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9LRS0.
PRIDEiQ9LRS0.

Expressioni

Gene expression databases

ExpressionAtlasiQ9LRS0. baseline and differential.

Interactioni

Subunit structurei

Homotetramer or homooctamer.By similarity

Protein-protein interaction databases

BioGridi5998. 5 interactions.
IntActiQ9LRS0. 1 interaction.
STRINGi3702.AT3G14415.2.

Structurei

3D structure databases

ProteinModelPortaliQ9LRS0.
SMRiQ9LRS0. Positions 1-359.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 359359FMN hydroxy acid dehydrogenasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi365 – 3673Microbody targeting signalSequence Analysis

Sequence similaritiesi

Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.PROSITE-ProRule annotation
Contains 1 FMN hydroxy acid dehydrogenase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG1304.
HOGENOMiHOG000217463.
InParanoidiQ9LRS0.
KOiK11517.
PhylomeDBiQ9LRS0.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
[Graphical view]
PfamiPF01070. FMN_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITEiPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q9LRS0-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEITNVTEYD AIAKAKLPKM VYDYYASGAE DQWTLQENRN AFARILFRPR
60 70 80 90 100
ILIDVNKIDM ATTVLGFKIS MPIMVAPTAF QKMAHPDGEY ATARAASAAG
110 120 130 140 150
TIMTLSSWAT SSVEEVASTG PGIRFFQLYV YKNRKVVEQL VRRAEKAGFK
160 170 180 190 200
AIALTVDTPR LGRRESDIKN RFTLPPNLTL KNFEGLDLGK MDEANDSGLA
210 220 230 240 250
SYVAGQIDRT LSWKDIQWLQ TITNMPILVK GVLTGEDARI AIQAGAAGII
260 270 280 290 300
VSNHGARQLD YVPATISALE EVVKATQGRV PVFLDGGVRR GTDVFKALAL
310 320 330 340 350
GASGIFIGRP VVFALAAEGE AGVKKVLQML RDEFELTMAL SGCRSLSEIT
360
RNHIVTEWDT PRHLPRL
Length:367
Mass (Da):40,307
Last modified:October 1, 2000 - v1
Checksum:iC0B0F9B083F1B6E6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028617, AB022220 Genomic DNA. Translation: BAB01333.1.
CP002686 Genomic DNA. Translation: AEE75515.1.
CP002686 Genomic DNA. Translation: AEE75517.1.
AY058095 mRNA. Translation: AAL24203.1.
AY136402 mRNA. Translation: AAM97068.1.
BT002129 mRNA. Translation: AAN72140.1.
AK221716 mRNA. Translation: BAD95441.1.
RefSeqiNP_001189892.1. NM_001202963.1. [Q9LRS0-1]
NP_188059.1. NM_112301.2. [Q9LRS0-1]
UniGeneiAt.20363.
At.67927.

Genome annotation databases

EnsemblPlantsiAT3G14415.1; AT3G14415.1; AT3G14415. [Q9LRS0-1]
AT3G14415.3; AT3G14415.3; AT3G14415. [Q9LRS0-1]
GeneIDi820664.
KEGGiath:AT3G14415.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028617, AB022220 Genomic DNA. Translation: BAB01333.1.
CP002686 Genomic DNA. Translation: AEE75515.1.
CP002686 Genomic DNA. Translation: AEE75517.1.
AY058095 mRNA. Translation: AAL24203.1.
AY136402 mRNA. Translation: AAM97068.1.
BT002129 mRNA. Translation: AAN72140.1.
AK221716 mRNA. Translation: BAD95441.1.
RefSeqiNP_001189892.1. NM_001202963.1. [Q9LRS0-1]
NP_188059.1. NM_112301.2. [Q9LRS0-1]
UniGeneiAt.20363.
At.67927.

3D structure databases

ProteinModelPortaliQ9LRS0.
SMRiQ9LRS0. Positions 1-359.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi5998. 5 interactions.
IntActiQ9LRS0. 1 interaction.
STRINGi3702.AT3G14415.2.

Proteomic databases

PaxDbiQ9LRS0.
PRIDEiQ9LRS0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G14415.1; AT3G14415.1; AT3G14415. [Q9LRS0-1]
AT3G14415.3; AT3G14415.3; AT3G14415. [Q9LRS0-1]
GeneIDi820664.
KEGGiath:AT3G14415.

Organism-specific databases

TAIRiAT3G14415.

Phylogenomic databases

eggNOGiCOG1304.
HOGENOMiHOG000217463.
InParanoidiQ9LRS0.
KOiK11517.
PhylomeDBiQ9LRS0.

Enzyme and pathway databases

UniPathwayiUPA00951; UER00912.
BioCyciARA:AT3G14415-MONOMER.
ARA:GQT-740-MONOMER.
ARA:GQT-741-MONOMER.
ReactomeiREACT_278920. Glyoxylate metabolism.

Miscellaneous databases

PROiQ9LRS0.

Gene expression databases

ExpressionAtlasiQ9LRS0. baseline and differential.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
[Graphical view]
PfamiPF01070. FMN_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITEiPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
    Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
    DNA Res. 7:131-135(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting peptides, metabolic pathways, and defense mechanisms."
    Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E., Rasche N., Lueder F., Weckwerth W., Jahn O.
    Plant Cell 19:3170-3193(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 240-257 AND 280-289, SUBCELLULAR LOCATION.
  6. "Proteomic analysis of leaf peroxisomal proteins in greening cotyledons of Arabidopsis thaliana."
    Fukao Y., Hayashi M., Nishimura M.
    Plant Cell Physiol. 43:689-696(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "Inducible antisense suppression of glycolate oxidase reveals its strong regulation over photosynthesis in rice."
    Xu H.-W., Zhang J., Zeng J., Jiang L., Liu E., Peng C., He Z.-H., Peng X.-X.
    J. Exp. Bot. 60:1799-1809(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.

Entry informationi

Entry nameiGLO2_ARATH
AccessioniPrimary (citable) accession number: Q9LRS0
Secondary accession number(s): Q56XF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: October 1, 2000
Last modified: June 24, 2015
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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.