B8B7C5 (GLO5_ORYSI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peroxisomal (S)-2-hydroxy-acid oxidase GLO5
EC=1.1.3.15

Alternative name(s):
Glycolate oxidase 5
Short name=GOX 5
Short name=OsGLO5
Short chain alpha-hydroxy acid oxidase GLO5

Gene names

Name:	GLO5
ORF Names:	OsI_24928

Organism

Oryza sativa subsp. indica (Rice)

Taxonomic identifier

39946 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Liliopsida › commelinids › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza › Oryza sativa

Protein attributes

Sequence length	369 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Glycolate pathway Host-virus interaction Photorespiration
Cellular component	Peroxisome
Ligand	FMN Flavoprotein
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological_process	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 virus-host interaction Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	apoplast 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_function	FMN 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 369	369	Peroxisomal (S)-2-hydroxy-acid oxidase GLO5		PRO_0000403418
Regions
	Domain	1 – 360	360	FMN hydroxy acid dehydrogenase
	Nucleotide binding	286 – 310	25	FMN By similarity
	Motif	367 – 369	3	Microbody targeting signal Potential
Sites
	Active site	255	1	Proton acceptor By similarity
	Binding site	25	1	Substrate Potential
	Binding site	107	1	FMN By similarity
	Binding site	128	1	FMN By similarity
	Binding site	130	1	Substrate By similarity
	Binding site	156	1	FMN By similarity
	Binding site	165	1	Substrate By similarity
	Binding site	231	1	FMN By similarity
	Binding site	258	1	Substrate Potential

Sequences

	Sequence		Length	Mass (Da)
	B8B7C5 [UniParc]. Last modified March 3, 2009. Version 1. Checksum: FE652FD1115F2681	FASTA	369	40,245
	10 20 30 40 50 60 MGEITNVTEY QAIAKQKLPK MIYDYYASGA EDEWTLQENR EAFARILFRP RILIDVSKID 70 80 90 100 110 120 MATTVLGFKI SMPIMIAPSA MQKMAHPDGE YATARAASAA GTIMTLSSWA TSSVEEVAST 130 140 150 160 170 180 GPGIRFFQLY VYKDRRVVEQ LVRRAERAGF KAIALTVDTP RLGRREADIK NRFVLPPFLT 190 200 210 220 230 240 LKNFEGLELG KMDQASDSGL ASYVAGQIDR TLSWKDVKWL QTITTLPILV KGVITAEDTR 250 260 270 280 290 300 LAVENGAAGI IVSNHGARQL DYVPATISAL EEVVKAARGQ LPVFLDGGVR RGTDVFKALA 310 320 330 340 350 360 LGAAGVFIGR PVVFSLAAAG EAGVRNVLQM LRDEFELTMA LSGCTSLADI TRNHVITEAD KLGVMPSRL

References

[1]

"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. , 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. 93-11.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CM000132 Genomic DNA. Translation: EEC81529.1.
3D structure databases
ProteinModelPortal	B8B7C5.
ModBase	Search...
Protein-protein interaction databases
STRING	39947.LOC_Os07g05820.2.
Proteomic databases
PRIDE	B8B7C5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
Gramene	B8B7C5.
Phylogenomic databases
eggNOG	COG1304.
HOGENOM	HOG000217463.
Enzyme and pathway databases
UniPathway	UPA00951; UER00912.
Gene expression databases
ArrayExpress	B8B7C5.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
InterPro	IPR013785. Aldolase_TIM. IPR012133. Alpha-hydoxy_acid_DH_FMN. IPR000262. FMN-dep_DH. IPR008259. FMN_hydac_DH_AS. [Graphical view]
Pfam	PF01070. FMN_dh. 1 hit. [Graphical view]
PIRSF	PIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITE	PS00557. FMN_HYDROXY_ACID_DH_1. 1 hit. PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLO5_ORYSI

Accession

Primary (citable) accession number: B8B7C5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2011
Last sequence update:	March 3, 2009
Last modified:	April 3, 2013
This is version 24 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program