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B8AKX6 (GLO1_ORYSI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
ORF Names:OsI_13800
OrganismOryza sativa subsp. indica (Rice)
Taxonomic identifier39946 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza

Protein attributes

Sequence length369 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity.

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. Interacts with rice dwarf virus (RDV) P8. This interaction promotes viral P8 relocation to virus factories peripheral to peroxisomes 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.

Ontologies

Keywords
   Biological processGlycolate pathway
Host-virus interaction
Photorespiration
   Cellular componentPeroxisome
   LigandFlavoprotein
FMN
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological_processdefense response signaling pathway, resistance gene-independent

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

defense 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 sequence or structural similarity. Source: UniProtKB

oxidative photosynthetic carbon pathway

Inferred from electronic annotation. Source: UniProtKB-UniPathway

photorespiration

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of photosynthesis

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentperoxisome

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionFMN binding

Inferred from electronic annotation. Source: InterPro

glycolate oxidase activity

Inferred from sequence or structural similarity. 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_0000403410

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
B8AKX6 [UniParc].

Last modified March 3, 2009. 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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CM000128 Genomic DNA. Translation: EEC76290.1.

3D structure databases

ProteinModelPortalB8AKX6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING39947.LOC_Os03g57220.2.

Proteomic databases

PRIDEB8AKX6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneB8AKX6.

Phylogenomic databases

eggNOGCOG1304.
HOGENOMHOG000217463.

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_ORYSI
AccessionPrimary (citable) accession number: B8AKX6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2011
Last sequence update: March 3, 2009
Last modified: April 16, 2014
This is version 29 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