Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P05414

- GOX_SPIOL

UniProt

P05414 - GOX_SPIOL

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Nov 1988)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

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

    Cofactori

    FMN.

    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

    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

    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 – 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.
    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

    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...
    MobiDBi 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: October 1, 2014
    This is version 110 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