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Protein

Peroxisomal (S)-2-hydroxy-acid oxidase

Gene
N/A
Organism
Spinacia oleracea (Spinach)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei24 – 241SubstratePROSITE-ProRule annotation
Binding sitei106 – 1061FMN1 PublicationPROSITE-ProRule annotation
Binding sitei127 – 1271FMN1 PublicationPROSITE-ProRule annotation
Binding sitei129 – 1291SubstratePROSITE-ProRule annotation
Binding sitei155 – 1551FMN1 PublicationPROSITE-ProRule annotation
Binding sitei164 – 1641SubstratePROSITE-ProRule annotation
Binding sitei230 – 2301FMN1 PublicationPROSITE-ProRule annotation
Active sitei254 – 2541Proton acceptor1 PublicationPROSITE-ProRule annotation
Binding sitei257 – 2571SubstratePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi285 – 30925FMN1 PublicationPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. FMN binding Source: InterPro
  2. long-chain-(S)-2-hydroxy-long-chain-acid oxidase activity Source: UniProtKB-EC
  3. medium-chain-(S)-2-hydroxy-acid oxidase activity Source: UniProtKB-EC
  4. very-long-chain-(S)-2-hydroxy-acid oxidase activity Source: UniProtKB-EC

GO - Biological processi

  1. oxidative photosynthetic carbon pathway Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolate pathway, Photorespiration

Keywords - Ligandi

Flavoprotein, FMN

Enzyme and pathway databases

UniPathwayiUPA00951; UER00912.

Names & Taxonomyi

Protein namesi
Recommended 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
OrganismiSpinacia oleracea (Spinach)
Taxonomic identifieri3562 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

Subcellular locationi

GO - Cellular componenti

  1. peroxisome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 369369Peroxisomal (S)-2-hydroxy-acid oxidasePRO_0000206325Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP05414.

Interactioni

Subunit structurei

Homotetramer or homooctamer.1 Publication

Structurei

Secondary structure

1
369
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 169Combined sources
Helixi19 – 268Combined sources
Helixi33 – 408Combined sources
Helixi41 – 444Combined sources
Beta strandi45 – 473Combined sources
Beta strandi62 – 643Combined sources
Beta strandi67 – 759Combined sources
Helixi81 – 833Combined sources
Helixi88 – 9811Combined sources
Beta strandi103 – 1053Combined sources
Helixi113 – 1197Combined sources
Beta strandi124 – 1285Combined sources
Beta strandi131 – 1333Combined sources
Helixi134 – 14613Combined sources
Beta strandi151 – 1555Combined sources
Helixi165 – 1695Combined sources
Helixi181 – 1833Combined sources
Beta strandi184 – 1863Combined sources
Helixi199 – 2057Combined sources
Helixi213 – 22210Combined sources
Beta strandi227 – 2304Combined sources
Helixi235 – 2439Combined sources
Beta strandi247 – 2515Combined sources
Helixi254 – 2563Combined sources
Beta strandi260 – 2623Combined sources
Helixi265 – 27511Combined sources
Turni276 – 2783Combined sources
Beta strandi282 – 2876Combined sources
Helixi291 – 2999Combined sources
Beta strandi305 – 3084Combined sources
Helixi309 – 32416Combined sources
Helixi328 – 3314Combined sources
Helixi339 – 3413Combined sources
Helixi346 – 3483Combined sources
Helixi351 – 3533Combined sources
Beta strandi354 – 3563Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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-ray1.35A176-195[»]
2A7NX-ray1.80A222-253[»]
2A7PX-ray2.20A176-195[»]
2A85X-ray2.50A176-195[»]
ProteinModelPortaliP05414.
SMRiP05414. Positions 1-359.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05414.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 359359FMN hydroxy acid dehydrogenasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi367 – 3693Microbody targeting signalSequence Analysis

Sequence similaritiesi

Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.PROSITE-ProRule annotation
Contains 1 FMN hydroxy acid dehydrogenase domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
[Graphical view]
PfamiPF01070. FMN_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITEiPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P05414-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEITNVNEYE AIAKQKLPKM VYDYYASGAE DQWTLAENRN AFSRILFRPR
60 70 80 90 100
ILIDVTNIDM TTTILGFKIS MPIMIAPTAM QKMAHPEGEY ATARAASAAG
110 120 130 140 150
TIMTLSSWAT SSVEEVASTG PGIRFFQLYV YKDRNVVAQL VRRAERAGFK
160 170 180 190 200
AIALTVDTPR LGRREADIKN RFVLPPFLTL KNFEGIDLGK MDKANDSGLS
210 220 230 240 250
SYVAGQIDRS LSWKDVAWLQ TITSLPILVK GVITAEDARL AVQHGAAGII
260 270 280 290 300
VSNHGARQLD YVPATIMALE EVVKAAQGRI PVFLDGGVRR GTDVFKALAL
310 320 330 340 350
GAAGVFIGRP VVFSLAAEGE AGVKKVLQMM RDEFELTMAL SGCRSLKEIS
360
RSHIAADWDG PSSRAVARL
Length:369
Mass (Da):40,286
Last modified:November 1, 1988 - v1
Checksum:i892F1B3D0C1B48E0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03492 mRNA. Translation: AAA34030.1.
PIRiA28496. OXSPH.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03492 mRNA. Translation: AAA34030.1.
PIRiA28496. OXSPH.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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-ray1.35A176-195[»]
2A7NX-ray1.80A222-253[»]
2A7PX-ray2.20A176-195[»]
2A85X-ray2.50A176-195[»]
ProteinModelPortaliP05414.
SMRiP05414. Positions 1-359.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP05414.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00951; UER00912.

Miscellaneous databases

EvolutionaryTraceiP05414.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
[Graphical view]
PfamiPF01070. FMN_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITEiPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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. 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.

Entry informationi

Entry nameiGOX_SPIOL
AccessioniPrimary (citable) accession number: P05414
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: March 4, 2015
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.