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Q10CE4 (GLO1_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 61. 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 GLO1

EC=1.1.3.15
Alternative name(s):
Glycolate oxidase 1
Short name=GOX 1
Short name=OsGLO1
Short chain alpha-hydroxy acid oxidase GLO1
Gene names
Name:GLO1
Synonyms:GOX
Ordered Locus Names:Os03g0786100, LOC_Os03g57220
ORF Names:OsJ_12861
OrganismOryza sativa subsp. japonica (Rice) [Reference proteome]
Taxonomic identifier39947 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza

Protein attributes

Sequence length369 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Photorespiratory enzyme that can exert a strong regulation over photosynthesis, possibly through a feed-back inhibition on Rubisco activase. Not required for oxalate accumulation. Ref.6 Ref.8

Catalytic activity

(S)-2-hydroxy acid + O2 = 2-oxo acid + H2O2. Ref.6

Cofactor

FMN By similarity.

Pathway

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

Subunit structure

Homotetramer or homooctamer By similarity. Interacts with rice dwarf virus (RDV) P8. This interaction promotes viral P8 relocation to virus factories peripheral to peroxisomes. Ref.7

Subcellular location

Peroxisome Ref.7.

Tissue specificity

Expressed constitutively in leaves (at protein level). Ref.6

Sequence similarities

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

Contains 1 FMN hydroxy acid dehydrogenase domain.

Biophysicochemical properties

Kinetic parameters:

KM=0.4 mM for glycolate (at pH 8.0 and 30 degrees Celsius) Ref.6

KM=4 mM for glyoxylate (at pH 8.0 and 30 degrees Celsius)

Ontologies

Keywords
   Biological processGlycolate pathway
Host-virus interaction
Photorespiration
   Cellular componentPeroxisome
   LigandFlavoprotein
FMN
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdefense response to bacterium

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

hydrogen peroxide biosynthetic process

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

modulation by virus of host morphology or physiology

Inferred from physical interaction Ref.7. Source: UniProtKB

oxidative photosynthetic carbon pathway

Inferred from electronic annotation. Source: UniProtKB-UniPathway

photorespiration

Inferred from mutant phenotype Ref.8. Source: UniProtKB

regulation of photosynthesis

Inferred from mutant phenotype Ref.8. Source: UniProtKB

   Cellular_componentapoplast

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

chloroplast stroma

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

cytosolic ribosome

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

membrane

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

nucleus

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

peroxisome

Inferred from direct assay Ref.7. Source: UniProtKB

plasmodesma

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Molecular_functionFMN binding

Inferred from electronic annotation. Source: InterPro

glycolate oxidase activity

Inferred from direct assay Ref.6. Source: UniProtKB

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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 369369Peroxisomal (S)-2-hydroxy-acid oxidase GLO1
PRO_0000403409

Regions

Domain1 – 360360FMN hydroxy acid dehydrogenase
Nucleotide binding286 – 31025FMN By similarity
Motif367 – 3693Microbody targeting signal Potential

Sites

Active site2551Proton acceptor By similarity
Binding site251Substrate Potential
Binding site1071FMN By similarity
Binding site1281FMN By similarity
Binding site1301Substrate By similarity
Binding site1561FMN By similarity
Binding site1651Substrate By similarity
Binding site2311FMN By similarity
Binding site2581Substrate Potential

Sequences

Sequence LengthMass (Da)Tools
Q10CE4 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: B14AF6A0E95883FF

FASTA36940,384
        10         20         30         40         50         60 
MGEITNVMEY QAIAKQKLPK MIYDYYASGA EDEWTLKENR EAFSRILFRP RILIDVSKID 

        70         80         90        100        110        120 
MSATVLGFKI SMPIMIAPSA MQKMAHPDGE YATARAASAA GTIMTLSSWA TSSVEEVAST 

       130        140        150        160        170        180 
GPGIRFFQLY VYKDRNVVEQ LVRRAERAGF KAIALTVDTP RLGRREADIK NRFVLPPYLT 

       190        200        210        220        230        240 
LKNFEGLDLA EMDKSNDSGL ASYVAGQIDR TLSWKDVKWL QSITSLPILV KGVITAEDAR 

       250        260        270        280        290        300 
LAVHSGAAGI IVSNHGARQL DYVPATISAL EEVVTAAAGR IPVYLDGGVR RGTDVFKALA 

       310        320        330        340        350        360 
LGAAGVFIGR PVVFALAAEG EAGVRNVLRM MREEFELTMA LSGCTSLADI TRAHIYTDAD 


RLARPFPRL 

« Hide

References

« Hide 'large scale' references
[1]"Sequence, annotation, and analysis of synteny between rice chromosome 3 and diverged grass species."
The rice chromosome 3 sequencing consortium
Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B., Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T., Fadrosh D., Bera J., Weaver B., Jin S. expand/collapse author list , Johri S., Reardon M., Webb K., Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T., Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R., Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J., Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S., Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M., Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M., Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L., O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R., Jin W., Lee H.R., Jiang J., Jackson S.
Genome Res. 15:1284-1291(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.
[2]"The map-based sequence of the rice genome."
International rice genome sequencing project (IRGSP)
Nature 436:793-800(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.
[3]"The rice annotation project database (RAP-DB): 2008 update."
The rice annotation project (RAP)
Nucleic Acids Res. 36:D1028-D1033(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: cv. Nipponbare.
[4]"The genomes of Oryza sativa: a history of duplications."
Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L. expand/collapse author list , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.
PLoS Biol. 3:266-281(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.
[5]"Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice."
The rice full-length cDNA consortium
Science 301:376-379(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Nipponbare.
[6]"Oxalate accumulation and regulation is independent of glycolate oxidase in rice leaves."
Xu H.-W., Ji X.-M., He Z.-H., Shi W.-P., Zhu G.-H., Niu J.-K., Li B.-S., Peng X.-X.
J. Exp. Bot. 57:1899-1908(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, FUNCTION.
Strain: cv. Shishoubaimao and cv. Xiangzhongxian 2.
[7]"Interaction of rice dwarf virus outer capsid P8 protein with rice glycolate oxidase mediates relocalization of P8."
Zhou F., Wu G., Deng W., Pu Y., Wei C., Li Y.
FEBS Lett. 581:34-40(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RICE DWARF VIRUS P8, SUBCELLULAR LOCATION.
Strain: cv. Xiushui 11.
[8]"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: FUNCTION, GENE FAMILY, NOMENCLATURE.
Strain: cv. Shishoubaimao.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DP000009 Genomic DNA. Translation: ABF99231.1.
AP008209 Genomic DNA. Translation: BAF13401.1.
CM000140 Genomic DNA. Translation: EEE60058.1.
AK098878 mRNA. Translation: BAG93788.1.
AK120304 mRNA. Translation: BAG99960.1.
RefSeqNP_001051487.1. NM_001058022.1.
UniGeneOs.74656.

3D structure databases

ProteinModelPortalQ10CE4.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ10CE4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsOS03T0786100-01; OS03T0786100-01; OS03G0786100.
OS03T0786100-02; OS03T0786100-02; OS03G0786100.
GeneID4334349.
KEGGosa:4334349.

Organism-specific databases

GrameneQ10CE4.

Phylogenomic databases

eggNOGCOG1304.
KOK11517.
OMARIYKDEL.
ProtClustDBCLSN2694368.

Enzyme and pathway databases

UniPathwayUPA00951; UER00912.

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_ORYSJ
AccessionPrimary (citable) accession number: Q10CE4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2011
Last sequence update: August 22, 2006
Last modified: April 16, 2014
This is version 61 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

Oryza sativa (rice)

Index of Oryza sativa entries and their corresponding gene designations

PATHWAY comments

Index of metabolic and biosynthesis pathways