Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9LRS0 (GLO2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:GLO2
Synonyms:GOX1
Ordered Locus Names:At3g14415
ORF Names:MLN21.20
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length367 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

FMN By similarity.

Pathway

Photosynthesis; photorespiration; glycine from 2-phosphoglycolate: step 2/3.

Subunit structure

Homotetramer or homooctamer By similarity.

Subcellular location

Peroxisome Ref.5 Ref.6.

Sequence similarities

Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.

Contains 1 FMN hydroxy acid dehydrogenase domain.

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q9LRS0-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 367367Peroxisomal (S)-2-hydroxy-acid oxidase GLO2
PRO_0000206323

Regions

Domain1 – 359359FMN hydroxy acid dehydrogenase
Nucleotide binding285 – 30925FMN By similarity
Motif365 – 3673Microbody targeting signal Potential

Sites

Active site2541Proton acceptor By similarity
Binding site241Substrate Potential
Binding site1061FMN By similarity
Binding site1271FMN By similarity
Binding site1291Substrate By similarity
Binding site1551FMN By similarity
Binding site1641Substrate By similarity
Binding site2301FMN By similarity
Binding site2571Substrate Potential

Amino acid modifications

Modified residue11N-acetylmethionine By similarity

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: C0B0F9B083F1B6E6

FASTA36740,307
        10         20         30         40         50         60 
MEITNVTEYD AIAKAKLPKM VYDYYASGAE DQWTLQENRN AFARILFRPR ILIDVNKIDM 

        70         80         90        100        110        120 
ATTVLGFKIS MPIMVAPTAF QKMAHPDGEY ATARAASAAG TIMTLSSWAT SSVEEVASTG 

       130        140        150        160        170        180 
PGIRFFQLYV YKNRKVVEQL VRRAEKAGFK AIALTVDTPR LGRRESDIKN RFTLPPNLTL 

       190        200        210        220        230        240 
KNFEGLDLGK MDEANDSGLA SYVAGQIDRT LSWKDIQWLQ TITNMPILVK GVLTGEDARI 

       250        260        270        280        290        300 
AIQAGAAGII VSNHGARQLD YVPATISALE EVVKATQGRV PVFLDGGVRR GTDVFKALAL 

       310        320        330        340        350        360 
GASGIFIGRP VVFALAAEGE AGVKKVLQML RDEFELTMAL SGCRSLSEIT RNHIVTEWDT 


PRHLPRL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001189892.1. NM_001202963.1. [Q9LRS0-1]
NP_188059.1. NM_112301.2. [Q9LRS0-1]
UniGeneAt.20363.
At.67927.

3D structure databases

ProteinModelPortalQ9LRS0.
SMRQ9LRS0. Positions 1-359.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid5998. 5 interactions.
IntActQ9LRS0. 1 interaction.
STRING3702.AT3G14415.1-P.

Proteomic databases

PaxDbQ9LRS0.
PRIDEQ9LRS0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G14415.1; AT3G14415.1; AT3G14415. [Q9LRS0-1]
AT3G14415.3; AT3G14415.3; AT3G14415. [Q9LRS0-1]
GeneID820664.
KEGGath:AT3G14415.

Organism-specific databases

TAIRAT3G14415.

Phylogenomic databases

eggNOGCOG1304.
HOGENOMHOG000217463.
InParanoidQ9LRS0.
KOK11517.
PhylomeDBQ9LRS0.

Enzyme and pathway databases

BioCycARA:AT3G14415-MONOMER.
ARA:GQT-740-MONOMER.
ARA:GQT-741-MONOMER.
UniPathwayUPA00951; UER00912.

Gene expression databases

GenevestigatorQ9LRS0.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
[Graphical view]
PfamPF01070. FMN_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITEPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLO2_ARATH
AccessionPrimary (citable) accession number: Q9LRS0
Secondary accession number(s): Q56XF8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names