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Q9LJH5 (GLO4_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 95. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxisomal (S)-2-hydroxy-acid oxidase GLO4

EC=1.1.3.15
Alternative name(s):
Glycolate oxidase 4
Short name=AtGLO4
Short name=GOX 4
Short chain alpha-hydroxy acid oxidase GLO4
Gene names
Name:GLO4
Ordered Locus Names:At3g14130
ORF Names:MAG2.2
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length363 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

Sequence similarities

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

Contains 1 FMN hydroxy acid dehydrogenase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 363363Peroxisomal (S)-2-hydroxy-acid oxidase GLO4
PRO_0000403407

Regions

Domain1 – 357357FMN hydroxy acid dehydrogenase
Nucleotide binding283 – 30725FMN By similarity
Motif361 – 3633Microbody targeting signal Potential

Sites

Active site2521Proton acceptor By similarity
Binding site1071FMN By similarity
Binding site1281FMN By similarity
Binding site1301Substrate By similarity
Binding site1561FMN By similarity
Binding site1651Substrate By similarity
Binding site2281FMN By similarity
Binding site2551Substrate Potential

Experimental info

Sequence conflict651M → I in AAM61594. Ref.4
Sequence conflict1071S → P in AAM61594. Ref.4
Sequence conflict2731A → V in AAM61594. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9LJH5 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 19A62CDD8F9E1088

FASTA36339,878
        10         20         30         40         50         60 
MDQIVNVDEF QELAKQALPK MYYDFYNGGA EDQHTLNENV QAFRRIMFRP RVLVDVSNID 

        70         80         90        100        110        120 
MSTSMLGYPI SAPIMIAPTA MHKLAHPKGE IATAKAAAAC NTIMIVSFMS TCTIEEVASS 

       130        140        150        160        170        180 
CNAVRFLQIY VYKRRDVTAQ IVKRAEKAGF KAIVLTVDVP RLGRREADIK NKMISPQLKN 

       190        200        210        220        230        240 
FEGLVSTEVR PNEGSGVEAF ASSAFDASLS WKDIEWLRSI TKLPILVKGL LTREDALKAV 

       250        260        270        280        290        300 
EAGVDGIVVS NHGARQLDYS PATITVLEEV VHAVKGRIPV LLDGGVRRGT DVFKALALGA 

       310        320        330        340        350        360 
QAVLIGRPIV YGLAAKGEDG VKKVIDMLKN EFEITMALSG CPTIDDVTRN HVRTENERIK 


SML 

« Hide

References

« Hide 'large scale' references
[1]"Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones."
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.
DNA Res. 7:217-221(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]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"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
AP000600 Genomic DNA. Translation: BAB02977.1.
CP002686 Genomic DNA. Translation: AEE75475.1.
BT002739 mRNA. Translation: AAO22568.1.
AY085037 mRNA. Translation: AAM61594.1.
RefSeqNP_188029.1. NM_112269.3.
UniGeneAt.39288.
At.42696.

3D structure databases

ProteinModelPortalQ9LJH5.
SMRQ9LJH5. Positions 3-355.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT3G14130.1-P.

Proteomic databases

PaxDbQ9LJH5.
PRIDEQ9LJH5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G14130.1; AT3G14130.1; AT3G14130.
GeneID820630.
KEGGath:AT3G14130.

Organism-specific databases

TAIRAT3G14130.

Phylogenomic databases

eggNOGCOG1304.
HOGENOMHOG000217463.
InParanoidQ9LJH5.
KOK11517.
OMAESCWVIV.
PhylomeDBQ9LJH5.

Enzyme and pathway databases

BioCycARA:AT3G14130-MONOMER.
UniPathwayUPA00951; UER00912.

Gene expression databases

GenevestigatorQ9LJH5.

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...

Other

PROQ9LJH5.

Entry information

Entry nameGLO4_ARATH
AccessionPrimary (citable) accession number: Q9LJH5
Secondary accession number(s): Q8LF60
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2011
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 95 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