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P05414 (GOX_SPIOL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 107. 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

EC=1.1.3.15
Alternative name(s):
Glycolate oxidase
Short name=GOX
Short chain alpha-hydroxy acid oxidase
OrganismSpinacia oleracea (Spinach)
Taxonomic identifier3562 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

Protein attributes

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

General annotation (Comments)

Catalytic activity

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

Cofactor

FMN.

Pathway

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

Subunit structure

Homotetramer or homooctamer.

Subcellular location

Peroxisome.

Sequence similarities

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

Contains 1 FMN hydroxy acid dehydrogenase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 369369Peroxisomal (S)-2-hydroxy-acid oxidase
PRO_0000206325

Regions

Domain1 – 359359FMN hydroxy acid dehydrogenase
Nucleotide binding285 – 30925FMN
Motif367 – 3693Microbody targeting signal Potential

Sites

Active site2541Proton acceptor Ref.3
Binding site241Substrate Potential
Binding site1061FMN
Binding site1271FMN
Binding site1291Substrate By similarity
Binding site1551FMN
Binding site1641Substrate By similarity
Binding site2301FMN
Binding site2571Substrate Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.2

Secondary structure

............................................................... 369
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05414 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: 892F1B3D0C1B48E0

FASTA36940,286
        10         20         30         40         50         60 
MEITNVNEYE AIAKQKLPKM VYDYYASGAE DQWTLAENRN AFSRILFRPR ILIDVTNIDM 

        70         80         90        100        110        120 
TTTILGFKIS MPIMIAPTAM QKMAHPEGEY ATARAASAAG TIMTLSSWAT SSVEEVASTG 

       130        140        150        160        170        180 
PGIRFFQLYV YKDRNVVAQL VRRAERAGFK AIALTVDTPR LGRREADIKN RFVLPPFLTL 

       190        200        210        220        230        240 
KNFEGIDLGK MDKANDSGLS SYVAGQIDRS LSWKDVAWLQ TITSLPILVK GVITAEDARL 

       250        260        270        280        290        300 
AVQHGAAGII VSNHGARQLD YVPATIMALE EVVKAAQGRI PVFLDGGVRR GTDVFKALAL 

       310        320        330        340        350        360 
GAAGVFIGRP VVFSLAAEGE AGVKKVLQMM RDEFELTMAL SGCRSLKEIS RSHIAADWDG 


PSSRAVARL 

« Hide

References

[1]"The primary structure of spinach glycolate oxidase deduced from the DNA sequence of a cDNA clone."
Volokita M., Somerville C.R.
J. Biol. Chem. 262:15825-15828(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Primary structure of glycolate oxidase from spinach."
Cederlund E., Lindqvist Y., Soederlund G., Braenden C.-I., Joernvall H.
Eur. J. Biochem. 173:523-530(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
[3]"The active site of spinach glycolate oxidase."
Lindqvist Y., Braenden C.-I.
J. Biol. Chem. 264:3624-3628(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE.
[4]"Refined structure of spinach glycolate oxidase at 2-A resolution."
Lindqvist Y.
J. Mol. Biol. 209:151-166(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[5]"Three-dimensional structures of glycolate oxidase with bound active-site inhibitors."
Stenberg K., Lindqvist Y.
Protein Sci. 6:1009-1015(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-359 IN COMPLEX WITH FMN AND INHIBITOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03492 mRNA. Translation: AAA34030.1.
PIROXSPH. A28496.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AL7X-ray2.60A1-359[»]
1AL8X-ray2.20A1-359[»]
1GOXX-ray2.00A1-369[»]
1GYLX-ray3.00A/B1-369[»]
1HUVX-ray2.15A176-195[»]
1P4CX-ray1.35A176-195[»]
1P5BX-ray1.35A112-195[»]
2A7NX-ray1.80A176-195[»]
2A7PX-ray2.20A176-195[»]
2A85X-ray2.50A176-195[»]
ProteinModelPortalP05414.
SMRP05414. Positions 1-359.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP05414.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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...

Other

EvolutionaryTraceP05414.

Entry information

Entry nameGOX_SPIOL
AccessionPrimary (citable) accession number: P05414
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: February 19, 2014
This is version 107 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways