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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: photorespiration

This protein is involved in step 2 of the subpathway that synthesizes glycine from 2-phosphoglycolate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Peroxisomal (S)-2-hydroxy-acid oxidase
  3. no protein annotated in this organism
This subpathway is part of the pathway photorespiration, which is itself part of Photosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes glycine from 2-phosphoglycolate, the pathway photorespiration and in Photosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei24SubstratePROSITE-ProRule annotation1
Binding sitei106FMNPROSITE-ProRule annotation1 Publication1
Binding sitei127FMNPROSITE-ProRule annotation1 Publication1
Binding sitei129SubstratePROSITE-ProRule annotation1
Binding sitei155FMNPROSITE-ProRule annotation1 Publication1
Binding sitei164SubstratePROSITE-ProRule annotation1
Binding sitei230FMNPROSITE-ProRule annotation1 Publication1
Active sitei254Proton acceptorPROSITE-ProRule annotation1 Publication1
Binding sitei257SubstratePROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi285 – 309FMNPROSITE-ProRule annotation1 PublicationAdd BLAST25

GO - Molecular functioni

GO - Biological processi

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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesChenopodiaceaeChenopodioideaeAnserineaeSpinacia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002063251 – 369Peroxisomal (S)-2-hydroxy-acid oxidaseAdd BLAST369

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP05414.

Interactioni

Subunit structurei

Homotetramer or homooctamer.1 Publication

Structurei

Secondary structure

1369
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 16Combined sources9
Helixi19 – 26Combined sources8
Helixi33 – 40Combined sources8
Helixi41 – 44Combined sources4
Beta strandi45 – 47Combined sources3
Beta strandi62 – 64Combined sources3
Beta strandi67 – 75Combined sources9
Helixi81 – 83Combined sources3
Helixi88 – 98Combined sources11
Beta strandi103 – 105Combined sources3
Helixi113 – 117Combined sources5
Beta strandi124 – 128Combined sources5
Beta strandi131 – 133Combined sources3
Helixi134 – 146Combined sources13
Beta strandi151 – 155Combined sources5
Helixi165 – 169Combined sources5
Helixi181 – 183Combined sources3
Beta strandi184 – 186Combined sources3
Helixi199 – 205Combined sources7
Helixi213 – 222Combined sources10
Beta strandi227 – 230Combined sources4
Helixi235 – 243Combined sources9
Beta strandi247 – 251Combined sources5
Helixi254 – 256Combined sources3
Beta strandi260 – 262Combined sources3
Helixi265 – 275Combined sources11
Turni276 – 278Combined sources3
Beta strandi282 – 287Combined sources6
Helixi291 – 300Combined sources10
Beta strandi303 – 307Combined sources5
Helixi309 – 341Combined sources33
Turni346 – 348Combined sources3
Helixi351 – 353Combined sources3
Beta strandi354 – 356Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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-ray1.80A176-195[»]
2A7PX-ray2.20A176-195[»]
2A85X-ray2.50A176-195[»]
ProteinModelPortaliP05414.
SMRiP05414.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05414.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 359FMN hydroxy acid dehydrogenasePROSITE-ProRule annotationAdd BLAST359

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi367 – 369Microbody targeting signalSequence analysis3

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
PDB 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-ray1.80A176-195[»]
2A7PX-ray2.20A176-195[»]
2A85X-ray2.50A176-195[»]
ProteinModelPortaliP05414.
SMRiP05414.
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...

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: November 2, 2016
This is version 124 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

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 one 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.