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Q9LRR9 (GLO1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. 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 GLO1

EC=1.1.3.15
Alternative name(s):
Glycolate oxidase 1
Short name=AtGLO1
Short name=GOX 1
Short chain alpha-hydroxy acid oxidase GLO1
Gene names
Name:GLO1
Ordered Locus Names:At3g14420
ORF Names:MAO2.2
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.

Sequence caution

The sequence AAL38298.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processGlycolate pathway
Photorespiration
   Cellular componentPeroxisome
   Coding sequence diversityAlternative splicing
   LigandFlavoprotein
FMN
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processdefense response to bacterium

Inferred from mutant phenotype PubMed 22286136. Source: TAIR

hydrogen peroxide biosynthetic process

Inferred from mutant phenotype PubMed 22286136. Source: TAIR

oxidative photosynthetic carbon pathway

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentapoplast

Inferred from direct assay PubMed 18538804. Source: TAIR

chloroplast

Inferred from direct assay PubMed 15028209PubMed 18431481. Source: TAIR

chloroplast stroma

Inferred from direct assay PubMed 18633119. Source: TAIR

cytosolic ribosome

Inferred from direct assay PubMed 15821981. Source: TAIR

membrane

Inferred from direct assay PubMed 17432890. Source: TAIR

nucleus

Inferred from direct assay PubMed 14617066. Source: TAIR

peroxisome

Inferred from direct assay Ref.5. Source: TAIR

plasmodesma

Inferred from direct assay PubMed 21533090. Source: TAIR

   Molecular_functionFMN binding

Inferred from electronic annotation. Source: InterPro

glycolate oxidase activity

Inferred from mutant phenotype PubMed 18685041. Source: TAIR

long-chain-(S)-2-hydroxy-long-chain-acid oxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

medium-chain-(S)-2-hydroxy-acid oxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

very-long-chain-(S)-2-hydroxy-acid oxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q9LRR9-1)

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.
Isoform 2 (identifier: Q9LRR9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 367367Peroxisomal (S)-2-hydroxy-acid oxidase GLO1
PRO_0000206324

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

Natural variations

Alternative sequence1 – 1919Missing in isoform 2.
VSP_040387

Experimental info

Sequence conflict551V → A in AAL16258. Ref.3
Sequence conflict3631P → L in AAL38298. Ref.3
Sequence conflict3631P → L in AAM10128. Ref.3

Sequences

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

Last modified October 1, 2000. Version 1.
Checksum: B107AD7AC983A04C

FASTA36740,341
        10         20         30         40         50         60 
MEITNVTEYD AIAKQKLPKM VYDYYASGAE DQWTLQENRN AFARILFRPR ILIDVSKIDM 

        70         80         90        100        110        120 
TTTVLGFKIS MPIMVAPTAM QKMAHPDGEY ATARAASAAG TIMTLSSWAT SSVEEVASTG 

       130        140        150        160        170        180 
PGIRFFQLYV YKNRNVVEQL VRRAERAGFK AIALTVDTPR LGRRESDIKN RFTLPPNLTL 

       190        200        210        220        230        240 
KNFEGLDLGK MDEANDSGLA SYVAGQIDRT LSWKDVQWLQ TITKLPILVK GVLTGEDARI 

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

       310        320        330        340        350        360 
GASGIFIGRP VVFSLAAEGE AGVRKVLQML RDEFELTMAL SGCRSLKEIS RNHITTEWDT 


PRPSARL 

« Hide

Isoform 2 [UniParc].

Checksum: 8A5904F8787FC515
Show »

FASTA34838,167

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] (ISOFORM 1).
Strain: cv. Columbia.
[4]"Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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, 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB028617 Genomic DNA. Translation: BAB01334.1.
CP002686 Genomic DNA. Translation: AEE75518.1.
CP002686 Genomic DNA. Translation: AEE75520.1.
CP002686 Genomic DNA. Translation: AEE75521.1.
AY053412 mRNA. Translation: AAK96642.1.
AF428396 mRNA. Translation: AAL16164.1.
AF428328 mRNA. Translation: AAL16258.1.
AY065122 mRNA. Translation: AAL38298.1. Different initiation.
AY074830 mRNA. Translation: AAL69528.1.
AY081566 mRNA. Translation: AAM10128.1.
AK317539 mRNA. Translation: BAH20203.1.
RefSeqNP_001030694.1. NM_001035617.1.
NP_188060.1. NM_112302.3.
NP_850584.1. NM_180253.1.
UniGeneAt.21768.
At.67007.
At.71586.

3D structure databases

ProteinModelPortalQ9LRR9.
SMRQ9LRR9. Positions 1-359.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid5999. 4 interactions.
IntActQ9LRR9. 2 interactions.

Proteomic databases

PaxDbQ9LRR9.
PRIDEQ9LRR9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G14420.1; AT3G14420.1; AT3G14420. [Q9LRR9-1]
AT3G14420.2; AT3G14420.2; AT3G14420. [Q9LRR9-1]
GeneID820665.
KEGGath:AT3G14420.

Organism-specific databases

TAIRAT3G14420.

Phylogenomic databases

eggNOGCOG1304.
HOGENOMHOG000217463.
InParanoidQ9LRR9.
KOK11517.
OMAMALVCVE.
PhylomeDBQ9LRR9.
ProtClustDBPLN02493.

Enzyme and pathway databases

BioCycARA:AT3G14420-MONOMER.
ARA:GQT-2237-MONOMER.
ARA:GQT-2238-MONOMER.
ARA:GQT-2239-MONOMER.
ARA:GQT-2240-MONOMER.
ARA:GQT-2241-MONOMER.
MetaCyc:AT3G14420-MONOMER.
UniPathwayUPA00951; UER00912.

Gene expression databases

GenevestigatorQ9LRR9.

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 nameGLO1_ARATH
AccessionPrimary (citable) accession number: Q9LRR9
Secondary accession number(s): B9DHI6, Q8VZA4, Q944K6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 114 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