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O49506 (GLO5_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxisomal (S)-2-hydroxy-acid oxidase GLO5

EC=1.1.3.15
Alternative name(s):
Glycolate oxidase 3
Short name=AtGLO5
Short name=GOX 3
Short chain alpha-hydroxy acid oxidase GLO5
Gene names
Name:GLO5
Synonyms:GOX3
Ordered Locus Names:At4g18360
ORF Names:F28J12.20
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length368 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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 Ref.4.

Sequence similarities

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

Contains 1 FMN hydroxy acid dehydrogenase domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O49506-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O49506-2)

The sequence of this isoform differs from the canonical sequence as follows:
     308-314: GRPSLFS → SSFIIYT
     315-368: Missing.
Note: Derived from EST data. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 368368Peroxisomal (S)-2-hydroxy-acid oxidase GLO5
PRO_0000403408

Regions

Domain1 – 359359FMN hydroxy acid dehydrogenase
Nucleotide binding285 – 30925FMN By similarity
Motif366 – 3683Microbody targeting signal Potential

Sites

Active site2541Proton acceptor By similarity
Binding site241Substrate Potential
Binding site1061FMN By similarity
Binding site1271FMN By similarity
Binding site1291Substrate By similarity
Binding site1551FMN By similarity
Binding site1641Substrate By similarity
Binding site2301FMN By similarity
Binding site2571Substrate Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.6

Natural variations

Alternative sequence308 – 3147GRPSLFS → SSFIIYT in isoform 2.
VSP_040388
Alternative sequence315 – 36854Missing in isoform 2.
VSP_040389

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 3B3B33BB0562F5AB

FASTA36840,482
        10         20         30         40         50         60 
MEITNVMEYE KIAKEKLPKM VYDYYASGAE DQWTLQENRN AFSRILFRPR ILIDVSKIDV 

        70         80         90        100        110        120 
STTVLGFNIS MPIMIAPTAM QKMAHPDGEL ATARATSAAG TIMTLSSWAT CSVEEVASTG 

       130        140        150        160        170        180 
PGIRFFQLYV YKDRNVVIQL VKRAEEAGFK AIALTVDTPR LGRRESDIKN RFALPRGLTL 

       190        200        210        220        230        240 
KNFEGLDLGK IDKTNDSGLA SYVAGQVDQS LSWKDIKWLQ SITSLPILVK GVITAEDARI 

       250        260        270        280        290        300 
AVEYGAAGII VSNHGARQLD YVPATIVALE EVVKAVEGRI PVFLDGGVRR GTDVFKALAL 

       310        320        330        340        350        360 
GASGVFVGRP SLFSLAADGE AGVRKMLQML RDEFELTMAL SGCRSLREIS RTHIKTDWDT 


PHYLSAKL 

« Hide

Isoform 2 [UniParc].

Checksum: 94F9E8721DFCC680
Show »

FASTA31434,404

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [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] (ISOFORM 1).
Strain: cv. Columbia.
[4]"Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting peptides, metabolic pathways, and defense mechanisms."
Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E., Rasche N., Lueder F., Weckwerth W., Jahn O.
Plant Cell 19:3170-3193(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[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.
[6]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL021710 Genomic DNA. Translation: CAA16716.1.
AL161548 Genomic DNA. Translation: CAB78838.1.
CP002687 Genomic DNA. Translation: AEE84031.1.
CP002687 Genomic DNA. Translation: AEE84032.1.
BT001945 mRNA. Translation: AAN71944.1.
PIRG85206.
T04532.
RefSeqNP_001078406.1. NM_001084937.1. [O49506-2]
NP_193570.1. NM_117946.2. [O49506-1]
UniGeneAt.24604.

3D structure databases

ProteinModelPortalO49506.
SMRO49506. Positions 1-359.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT4G18360.1-P.

Proteomic databases

PaxDbO49506.
PRIDEO49506.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G18360.1; AT4G18360.1; AT4G18360. [O49506-1]
GeneID827563.
KEGGath:AT4G18360.

Organism-specific databases

TAIRAT4G18360.

Phylogenomic databases

eggNOGCOG1304.
HOGENOMHOG000217463.
InParanoidO49506.
KOK11517.
OMAARIAVEY.
PhylomeDBO49506.

Enzyme and pathway databases

BioCycARA:AT4G18360-MONOMER.
RETL1328306-WGS:GSTH-433-MONOMER.
UniPathwayUPA00951; UER00912.

Gene expression databases

GenevestigatorO49506.

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 nameGLO5_ARATH
AccessionPrimary (citable) accession number: O49506
Secondary accession number(s): A8MRC3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2011
Last sequence update: June 1, 1998
Last modified: July 9, 2014
This is version 103 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