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P05414

- GOX_SPIOL

UniProt

P05414 - GOX_SPIOL

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Protein
Peroxisomal (S)-2-hydroxy-acid oxidase
Gene
N/A
Organism
Spinacia oleracea (Spinach)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

FMN.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei24 – 241Substrate Reviewed prediction
Binding sitei106 – 1061FMN
Binding sitei127 – 1271FMN
Binding sitei129 – 1291Substrate By similarity
Binding sitei155 – 1551FMN
Binding sitei164 – 1641Substrate By similarity
Binding sitei230 – 2301FMN
Active sitei254 – 2541Proton acceptor1 Publication
Binding sitei257 – 2571Substrate Reviewed prediction

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi285 – 30925FMN
Add
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
Complete GO annotation...

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 oxidase
PRO_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.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 169
Helixi19 – 268
Helixi33 – 408
Helixi41 – 444
Beta strandi45 – 473
Beta strandi62 – 643
Beta strandi67 – 759
Helixi81 – 833
Helixi88 – 9811
Beta strandi103 – 1053
Helixi113 – 1175
Beta strandi124 – 1285
Beta strandi131 – 1333
Helixi134 – 14613
Beta strandi151 – 1555
Helixi165 – 1695
Helixi181 – 1833
Beta strandi184 – 1863
Helixi199 – 2057
Helixi213 – 22210
Beta strandi227 – 2304
Helixi235 – 2439
Beta strandi247 – 2515
Helixi254 – 2563
Beta strandi260 – 2623
Helixi265 – 27511
Turni276 – 2783
Beta strandi282 – 2876
Helixi291 – 30010
Beta strandi303 – 3075
Helixi309 – 34133
Turni346 – 3483
Helixi351 – 3533
Beta strandi354 – 3563

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AL7X-ray2.60A1-359[»]
1AL8X-ray2.20A1-359[»]
1GOXX-ray2.00A1-369[»]
1GYLX-ray3.00A/B1-369[»]
1HUVX-ray2.15A67-255[»]
A284-369[»]
1P4CX-ray1.35A176-195[»]
1P5BX-ray1.35A176-195[»]
2A7NX-ray1.80A176-195[»]
2A7PX-ray2.20A176-195[»]
2A85X-ray2.50A176-195[»]
ProteinModelPortaliP05414.
SMRiP05414. Positions 1-359.

Miscellaneous databases

EvolutionaryTraceiP05414.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 359359FMN hydroxy acid dehydrogenase
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi367 – 3693Microbody targeting signal Reviewed prediction

Sequence similaritiesi

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

MEITNVNEYE AIAKQKLPKM VYDYYASGAE DQWTLAENRN AFSRILFRPR    50
ILIDVTNIDM TTTILGFKIS MPIMIAPTAM QKMAHPEGEY ATARAASAAG 100
TIMTLSSWAT SSVEEVASTG PGIRFFQLYV YKDRNVVAQL VRRAERAGFK 150
AIALTVDTPR LGRREADIKN RFVLPPFLTL KNFEGIDLGK MDKANDSGLS 200
SYVAGQIDRS LSWKDVAWLQ TITSLPILVK GVITAEDARL AVQHGAAGII 250
VSNHGARQLD YVPATIMALE EVVKAAQGRI PVFLDGGVRR GTDVFKALAL 300
GAAGVFIGRP VVFSLAAEGE AGVKKVLQMM RDEFELTMAL SGCRSLKEIS 350
RSHIAADWDG PSSRAVARL 369
Length:369
Mass (Da):40,286
Last modified:November 1, 1988 - v1
Checksum:i892F1B3D0C1B48E0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03492 mRNA. Translation: AAA34030.1.
PIRiA28496. OXSPH.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03492 mRNA. Translation: AAA34030.1 .
PIRi A28496. OXSPH.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AL7 X-ray 2.60 A 1-359 [» ]
1AL8 X-ray 2.20 A 1-359 [» ]
1GOX X-ray 2.00 A 1-369 [» ]
1GYL X-ray 3.00 A/B 1-369 [» ]
1HUV X-ray 2.15 A 67-255 [» ]
A 284-369 [» ]
1P4C X-ray 1.35 A 176-195 [» ]
1P5B X-ray 1.35 A 176-195 [» ]
2A7N X-ray 1.80 A 176-195 [» ]
2A7P X-ray 2.20 A 176-195 [» ]
2A85 X-ray 2.50 A 176-195 [» ]
ProteinModelPortali P05414.
SMRi P05414. Positions 1-359.
ModBasei Search...

Proteomic databases

PRIDEi P05414.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00951 ; UER00912 .

Miscellaneous databases

EvolutionaryTracei P05414.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
[Graphical view ]
Pfami PF01070. FMN_dh. 1 hit.
[Graphical view ]
PIRSFi PIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITEi PS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 109 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

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