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Q7XPR4 (GLO2_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peroxisomal (S)-2-hydroxy-acid oxidase GLO2
EC=1.1.3.15
Alternative name(s):
Glycolate oxidase 2
Short name=GOX 2
Short name=OsGLO2
Short chain alpha-hydroxy acid oxidase GLO2
Gene names
Name:GLO2
Ordered Locus Names:Os04g0623600, LOC_Os04g53214
ORF Names:OsJ_16218, OSJNBa0053K19.9
OrganismOryza sativa subsp. japonica (Rice) [Reference proteome]
Taxonomic identifier39947 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza ›

Protein attributes

Sequence length368 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 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.

Sequence caution

The sequence CAE03501.2 differs from that shown. Reason: Erroneous gene model prediction.

The sequence EEE61717.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processGlycolate pathway
Host-virus interaction
Photorespiration
   Cellular componentPeroxisome
   LigandFMN
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processoxidative 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

virus-host interaction

Inferred from sequence or structural similarity. 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 sequence or structural similarity. Source: UniProtKB

vacuole

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   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: EC

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

Inferred from electronic annotation. Source: EC

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

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 368368Peroxisomal (S)-2-hydroxy-acid oxidase GLO2
PRO_0000403411

Regions

Domain1 – 360360FMN hydroxy acid dehydrogenase
Nucleotide binding286 – 31025FMN By similarity
Motif366 – 3683Microbody targeting signal Potential

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q7XPR4 [UniParc].

Last modified January 11, 2011. Version 3.
Checksum: 51A836116454D1F2

FASTA36840,593
        10         20         30         40         50         60 
MALVTNVCEY EELAKHKLPK MVYDFYAVDA EDQWTLRENS EAFSRILFQP VVLVDVSCID 

        70         80         90        100        110        120 
MSMSVLGYNI SMPIMIAPTA LHKLAHPEGE LATARAAAAA ETIMTLSSWS SCSIEEVNLA 

       130        140        150        160        170        180 
GPGVRFFQLS IYKDRNLVQQ LIQRAEKAGY KAIVLTVDAP WLGRREADVK NRFTLPQNVM 

       190        200        210        220        230        240 
LKIFEGLDQG KIDETNGSGL AAYVASQIDR SFSWKDIKWL QTVTSLPVLV KGIITAQDTR 

       250        260        270        280        290        300 
IAIEYGAAGI IMSNHGGRQL DYLPATISCL EEVVREANGR VPVFIDSGFR RGTDVFKALA 

       310        320        330        340        350        360 
LGASGVFIGR PVLFSLAIDG EAGVRNALRM LRDELEITMA LSGCTSVKEI TRGHVVTESD 


RIRRCSRL

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of rice chromosome 4."
Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y., Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q., Zhang L. expand/collapse author list , Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T., Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R., Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G., Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C., Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J., Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J., Li J., Hong G., Xue Y., Han B.
Nature 420:316-320(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.
[2]"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.
[3]"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		AL606645 Genomic DNA. Translation: CAE03501.2. Sequence problems.
CM000141 Genomic DNA. Translation: EEE61717.1. Sequence problems.

3D structure databases

HSSPHSSP built from PDB template 1GOX based on UniProtKB P05414.
ProteinModelPortalQ7XPR4.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsLOC_Os04g53214.2; LOC_Os04g53214.2; LOC_Os04g53214.
KEGGdosa:Os04t0623600-01.

Organism-specific databases

GrameneQ7XPR4.

Phylogenomic databases

eggNOGCOG1304.

Enzyme and pathway databases

UniPathwayUPA00951; UER00912.

Gene expression databases

ArrayExpressQ7XPR4.

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_ORYSJ
AccessionPrimary (citable) accession number: Q7XPR4
Secondary accession number(s): B9FCL2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2011
Last sequence update: January 11, 2011
Last modified: April 3, 2013
This is version 49 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Oryza sativa (rice)

Index of Oryza sativa entries and their corresponding gene designations

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents