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Protein

Galactose oxidase

Gene

GAOA

Organism
Gibberella zeae (Wheat head blight fungus) (Fusarium graminearum)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the sterospecific oxidation of primary alcohols to the corresponding aldehydes. The biologically relevant substrate of the enzyme is not known as the enzyme exhibits broad substrate specificity from small alcohols through sugars to oligo- and polysaccharides.2 Publications

Catalytic activityi

D-galactose + O2 = D-galacto-hexodialdose + H2O2.

Cofactori

Cu2+Note: Binds 1 Cu2+ ion per subunit.

Enzyme regulationi

Inhibited by diethyldithiocarbamate.1 Publication

Kineticsi

  1. KM=56 mM for 1-methyl-alpha-D-galactopyranoside5 Publications
  2. KM=57 mM for 2-methylene-1,3-propanediol5 Publications
  3. KM=68 mM for D-galactose5 Publications
  4. KM=2.5 M for D-fructose5 Publications

    pH dependencei

    Optimum pH is 7. Active from pH 5.7 to 9.4.5 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi313Copper1
    Active sitei536Proton acceptor1 Publication1
    Metal bindingi536Copper1
    Metal bindingi537Copper1
    Metal bindingi622Copper1

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Copper, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-15357.
    SABIO-RKP0CS93.

    Protein family/group databases

    CAZyiAA5. Auxiliary Activities 5.
    CBM32. Carbohydrate-Binding Module Family 32.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Galactose oxidase (EC:1.1.3.9)
    Short name:
    GAO
    Short name:
    GO
    Short name:
    GOase
    Gene namesi
    Name:GAOA
    OrganismiGibberella zeae (Wheat head blight fungus) (Fusarium graminearum)
    Taxonomic identifieri5518 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusarium

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi269C → G: Reduces catalytic activity more than 10000-fold. 1
    Mutagenesisi331W → F: Reduces catalytic efficiency 50-fold and substrate affinity 36-fold. 1
    Mutagenesisi331W → G: Reduces substrate affinity 20-fold and catalytic activity more than 6000-fold. 1
    Mutagenesisi331W → H: Reduces catalytic efficiency 1000-fold. 1
    Mutagenesisi371R → A: Reduces catalytic efficiency 250-fold and substrate affinity 22-fold for D-galactose, but improves catalytic efficiency 1.8-fold towards D-fructose. 1 Publication1
    Mutagenesisi371R → K: Reduces catalytic efficiency 45-fold and substrate affinity 8.7-fold for D-galactose, but improves catalytic efficiency 8-fold towards D-fructose. 1 Publication1
    Mutagenesisi424C → A: Reduces catalytic efficiency 1.5-to 2-fold towards D-galactose and 1-methyl-alpha-D-galactopyranoside. 1 Publication1
    Mutagenesisi424C → S: Improves catalytic efficiency 3- to 4-fold towards D-galactose and 1-methyl-alpha-D-galactopyranoside, mainly by increasing the affinity for the substrates. Improves catalytic efficiency 5.3-fold towards D-galactose; when associated with H-477. Improves catalytic efficiency 4.9-fold towards 1-methyl-alpha-D-galactopyranoside; when associated with A-535. Improves catalytic activity 4.7-fold towards D-galactose, but only 1.8-fold towards 1-methyl-alpha-D-galactopyranoside; when associated with A-477. 1 Publication1
    Mutagenesisi477Y → A: No effect. Improves catalytic efficiency 2- to 3-fold towards D-galactose and 1-methyl-alpha-D-galactopyranoside; when associated with A-535. Improves catalytic activity 4.7-fold towards D-galactose, but only 1.8-fold towards 1-methyl-alpha-D-galactopyranoside; when associated with S-424. 1 Publication1
    Mutagenesisi477Y → H: No effect. Improves catalytic efficiency 5.3-fold towards D-galactose; when associated with S-424. 1 Publication1
    Mutagenesisi505F → A: Reduces catalytic efficiency 166-fold and substrate affinity 9-fold. 1 Publication1
    Mutagenesisi535V → A: Improves catalytic efficiency 1.3-to 1.8-fold. Improves catalytic efficiency 2- to 3-fold towards D-galactose and 1-methyl-alpha-D-galactopyranoside; when associated with A-477. Improves catalytic efficiency 4.9-fold towards 1-methyl-alpha-D-galactopyranoside; when associated with S-424. 1 Publication1
    Mutagenesisi536Y → F: Reduces catalytic efficiency 1000-fold, but does not reduce substrate affinity. 1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 241 PublicationAdd BLAST24
    PropeptideiPRO_000028540725 – 412 PublicationsAdd BLAST17
    ChainiPRO_000001661042 – 680Galactose oxidaseAdd BLAST639

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi59 ↔ 68
    Cross-linki269 ↔ 3133'-(S-cysteinyl)-tyrosine (Cys-Tyr)
    Disulfide bondi556 ↔ 559

    Post-translational modificationi

    Galactose oxidase contains a protein-derived free radical cofactor. In the active state, Tyr-313, which is cross-linked to Cys-269 via a thioether bond, is oxidized to a radical and acts with Cu2+ as a two-electron acceptor in the oxidation reaction. The cross-link is believed to modulate the redox potential of the tyrosyl radical, which is further stabilized by a stacking interaction with Trp-331 in the active site. The post-translational formation of the cross-link is closely linked to the propeptide cleavage event, and both are copper-dependent, autocatalytic processes. The propeptide may act as an intramolecular chaperone, facilitating thioester bond formation and copper binding by positioning of active-site residues, including copper ligands.

    Keywords - PTMi

    Disulfide bond, Thioether bond

    Interactioni

    Subunit structurei

    Monomer.6 Publications

    Structurei

    Secondary structure

    1680
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi35 – 37Combined sources3
    Beta strandi46 – 49Combined sources4
    Beta strandi56 – 60Combined sources5
    Helixi68 – 71Combined sources4
    Beta strandi72 – 74Combined sources3
    Helixi85 – 87Combined sources3
    Beta strandi94 – 112Combined sources19
    Beta strandi125 – 135Combined sources11
    Beta strandi141 – 145Combined sources5
    Beta strandi148 – 151Combined sources4
    Beta strandi153 – 169Combined sources17
    Beta strandi180 – 188Combined sources9
    Beta strandi201 – 207Combined sources7
    Beta strandi213 – 217Combined sources5
    Turni219 – 221Combined sources3
    Beta strandi224 – 229Combined sources6
    Turni233 – 235Combined sources3
    Beta strandi241 – 248Combined sources8
    Turni250 – 252Combined sources3
    Beta strandi259 – 262Combined sources4
    Beta strandi271 – 274Combined sources4
    Beta strandi280 – 283Combined sources4
    Beta strandi285 – 287Combined sources3
    Beta strandi291 – 295Combined sources5
    Turni296 – 299Combined sources4
    Beta strandi300 – 303Combined sources4
    Beta strandi315 – 318Combined sources4
    Beta strandi324 – 327Combined sources4
    Beta strandi333 – 335Combined sources3
    Beta strandi340 – 344Combined sources5
    Turni345 – 348Combined sources4
    Beta strandi349 – 353Combined sources5
    Helixi359 – 361Combined sources3
    Helixi368 – 370Combined sources3
    Turni371 – 373Combined sources3
    Beta strandi378 – 380Combined sources3
    Helixi382 – 384Combined sources3
    Beta strandi386 – 388Combined sources3
    Beta strandi391 – 399Combined sources9
    Beta strandi405 – 411Combined sources7
    Beta strandi426 – 431Combined sources6
    Turni432 – 435Combined sources4
    Beta strandi436 – 440Combined sources5
    Beta strandi443 – 450Combined sources8
    Beta strandi455 – 459Combined sources5
    Beta strandi468 – 471Combined sources4
    Beta strandi480 – 482Combined sources3
    Beta strandi484 – 487Combined sources4
    Beta strandi493 – 496Combined sources4
    Beta strandi499 – 501Combined sources3
    Beta strandi515 – 518Combined sources4
    Helixi519 – 521Combined sources3
    Beta strandi523 – 526Combined sources4
    Beta strandi538 – 542Combined sources5
    Beta strandi548 – 552Combined sources5
    Beta strandi565 – 570Combined sources6
    Helixi572 – 574Combined sources3
    Beta strandi579 – 581Combined sources3
    Beta strandi587 – 591Combined sources5
    Beta strandi593 – 596Combined sources4
    Beta strandi600 – 607Combined sources8
    Beta strandi610 – 616Combined sources7
    Beta strandi619 – 621Combined sources3
    Beta strandi630 – 632Combined sources3
    Beta strandi635 – 639Combined sources5
    Beta strandi642 – 646Combined sources5
    Turni651 – 653Combined sources3
    Beta strandi656 – 664Combined sources9
    Beta strandi674 – 679Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1GOFX-ray1.70A42-680[»]
    1GOGX-ray1.90A42-680[»]
    1GOHX-ray2.20A42-680[»]
    1K3IX-ray1.40A25-680[»]
    1T2XX-ray2.30A42-680[»]
    2EIBX-ray2.10A42-680[»]
    2EICX-ray2.80A42-680[»]
    2EIDX-ray2.20A42-680[»]
    2EIEX-ray1.80A42-680[»]
    2JKXX-ray1.84A42-680[»]
    2VZ1X-ray1.91A42-680[»]
    2VZ3X-ray1.90A42-680[»]
    2WQ8X-ray2.19A42-680[»]
    ProteinModelPortaliP0CS93.
    SMRiP0CS93.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini42 – 189F5/8 type CPROSITE-ProRule annotationAdd BLAST148
    Repeati223 – 268Kelch 1Add BLAST46
    Repeati279 – 321Kelch 2Add BLAST43
    Repeati323 – 372Kelch 3Add BLAST50
    Repeati436 – 490Kelch 4Add BLAST55
    Repeati492 – 544Kelch 5Add BLAST53

    Sequence similaritiesi

    Contains 1 F5/8 type C domain.PROSITE-ProRule annotation
    Contains 5 Kelch repeats.Curated

    Keywords - Domaini

    Kelch repeat, Repeat, Signal

    Phylogenomic databases

    eggNOGiENOG410IJM5. Eukaryota.
    ENOG410XSZ3. LUCA.

    Family and domain databases

    CDDicd02851. E_set_GO_C. 1 hit.
    Gene3Di2.130.10.80. 1 hit.
    2.60.120.260. 1 hit.
    2.60.40.10. 1 hit.
    InterProiIPR015202. DUF1929.
    IPR000421. FA58C.
    IPR011043. Gal_Oxase/kelch_b-propeller.
    IPR015916. Gal_Oxidase_b-propeller.
    IPR008979. Galactose-bd-like.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR006652. Kelch_1.
    [Graphical view]
    PfamiPF09118. DUF1929. 1 hit.
    PF00754. F5_F8_type_C. 1 hit.
    PF01344. Kelch_1. 1 hit.
    [Graphical view]
    SMARTiSM00231. FA58C. 1 hit.
    SM00612. Kelch. 3 hits.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 1 hit.
    SSF50965. SSF50965. 1 hit.
    SSF81296. SSF81296. 1 hit.
    PROSITEiPS50022. FA58C_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0CS93-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKHLLTLALC FSSINAVAVT VPHKAVGTGI PEGSLQFLSL RASAPIGSAI
    60 70 80 90 100
    SRNNWAVTCD SAQSGNECNK AIDGNKDTFW HTFYGANGDP KPPHTYTIDM
    110 120 130 140 150
    KTTQNVNGLS MLPRQDGNQN GWIGRHEVYL SSDGTNWGSP VASGSWFADS
    160 170 180 190 200
    TTKYSNFETR PARYVRLVAI TEANGQPWTS IAEINVFQAS SYTAPQPGLG
    210 220 230 240 250
    RWGPTIDLPI VPAAAAIEPT SGRVLMWSSY RNDAFGGSPG GITLTSSWDP
    260 270 280 290 300
    STGIVSDRTV TVTKHDMFCP GISMDGNGQI VVTGGNDAKK TSLYDSSSDS
    310 320 330 340 350
    WIPGPDMQVA RGYQSSATMS DGRVFTIGGS WSGGVFEKNG EVYSPSSKTW
    360 370 380 390 400
    TSLPNAKVNP MLTADKQGLY RSDNHAWLFG WKKGSVFQAG PSTAMNWYYT
    410 420 430 440 450
    SGSGDVKSAG KRQSNRGVAP DAMCGNAVMY DAVKGKILTF GGSPDYQDSD
    460 470 480 490 500
    ATTNAHIITL GEPGTSPNTV FASNGLYFAR TFHTSVVLPD GSTFITGGQR
    510 520 530 540 550
    RGIPFEDSTP VFTPEIYVPE QDTFYKQNPN SIVRVYHSIS LLLPDGRVFN
    560 570 580 590 600
    GGGGLCGDCT TNHFDAQIFT PNYLYNSNGN LATRPKITRT STQSVKVGGR
    610 620 630 640 650
    ITISTDSSIS KASLIRYGTA THTVNTDQRR IPLTLTNNGG NSYSFQVPSD
    660 670 680
    SGVALPGYWM LFVMNSAGVP SVASTIRVTQ
    Length:680
    Mass (Da):72,823
    Last modified:July 11, 2012 - v1
    Checksum:i2F97C561B63E46E9
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti111M → I in AAB94635 (Ref. 4) Curated1

    Mass spectrometryi

    Molecular mass is 68520 Da from positions 42 - 680. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M86819 Unassigned DNA. Translation: AAA16228.1.
    AH005781 Genomic DNA. Translation: AAB94635.1.

    Cross-referencesi

    Web resourcesi

    Worthington enzyme manual

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M86819 Unassigned DNA. Translation: AAA16228.1.
    AH005781 Genomic DNA. Translation: AAB94635.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1GOFX-ray1.70A42-680[»]
    1GOGX-ray1.90A42-680[»]
    1GOHX-ray2.20A42-680[»]
    1K3IX-ray1.40A25-680[»]
    1T2XX-ray2.30A42-680[»]
    2EIBX-ray2.10A42-680[»]
    2EICX-ray2.80A42-680[»]
    2EIDX-ray2.20A42-680[»]
    2EIEX-ray1.80A42-680[»]
    2JKXX-ray1.84A42-680[»]
    2VZ1X-ray1.91A42-680[»]
    2VZ3X-ray1.90A42-680[»]
    2WQ8X-ray2.19A42-680[»]
    ProteinModelPortaliP0CS93.
    SMRiP0CS93.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    CAZyiAA5. Auxiliary Activities 5.
    CBM32. Carbohydrate-Binding Module Family 32.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    eggNOGiENOG410IJM5. Eukaryota.
    ENOG410XSZ3. LUCA.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-15357.
    SABIO-RKP0CS93.

    Family and domain databases

    CDDicd02851. E_set_GO_C. 1 hit.
    Gene3Di2.130.10.80. 1 hit.
    2.60.120.260. 1 hit.
    2.60.40.10. 1 hit.
    InterProiIPR015202. DUF1929.
    IPR000421. FA58C.
    IPR011043. Gal_Oxase/kelch_b-propeller.
    IPR015916. Gal_Oxidase_b-propeller.
    IPR008979. Galactose-bd-like.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR006652. Kelch_1.
    [Graphical view]
    PfamiPF09118. DUF1929. 1 hit.
    PF00754. F5_F8_type_C. 1 hit.
    PF01344. Kelch_1. 1 hit.
    [Graphical view]
    SMARTiSM00231. FA58C. 1 hit.
    SM00612. Kelch. 3 hits.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 1 hit.
    SSF50965. SSF50965. 1 hit.
    SSF81296. SSF81296. 1 hit.
    PROSITEiPS50022. FA58C_3. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiGAOA_GIBZA
    AccessioniPrimary (citable) accession number: P0CS93
    Secondary accession number(s): O43098, Q01745, Q4HVH6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2012
    Last sequence update: July 11, 2012
    Last modified: November 2, 2016
    This is version 23 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Caution

    Was originally thought to originate from Polyporus circinatus then later from Dactylium dendroides and is now known to be originating from Gibberella (Fusarium).Curated

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. 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.