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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)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi313 – 3131Copper
    Active sitei536 – 5361Proton acceptor1 Publication
    Metal bindingi536 – 5361Copper
    Metal bindingi537 – 5371Copper
    Metal bindingi622 – 6221Copper

    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

    CAZyiCBM32. 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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi269 – 2691C → G: Reduces catalytic activity more than 10000-fold.
    Mutagenesisi331 – 3311W → F: Reduces catalytic efficiency 50-fold and substrate affinity 36-fold.
    Mutagenesisi331 – 3311W → G: Reduces substrate affinity 20-fold and catalytic activity more than 6000-fold.
    Mutagenesisi331 – 3311W → H: Reduces catalytic efficiency 1000-fold.
    Mutagenesisi371 – 3711R → 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 Publication
    Mutagenesisi371 – 3711R → 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 Publication
    Mutagenesisi424 – 4241C → A: Reduces catalytic efficiency 1.5-to 2-fold towards D-galactose and 1-methyl-alpha-D-galactopyranoside. 1 Publication
    Mutagenesisi424 – 4241C → 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 Publication
    Mutagenesisi477 – 4771Y → 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 Publication
    Mutagenesisi477 – 4771Y → H: No effect. Improves catalytic efficiency 5.3-fold towards D-galactose; when associated with S-424. 1 Publication
    Mutagenesisi505 – 5051F → A: Reduces catalytic efficiency 166-fold and substrate affinity 9-fold. 1 Publication
    Mutagenesisi535 – 5351V → 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 Publication
    Mutagenesisi536 – 5361Y → F: Reduces catalytic efficiency 1000-fold, but does not reduce substrate affinity.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 24241 PublicationAdd
    BLAST
    Propeptidei25 – 41172 PublicationsPRO_0000285407Add
    BLAST
    Chaini42 – 680639Galactose oxidasePRO_0000016610Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    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

    1
    680
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi35 – 373Combined sources
    Beta strandi46 – 494Combined sources
    Beta strandi56 – 605Combined sources
    Helixi68 – 714Combined sources
    Beta strandi72 – 743Combined sources
    Helixi85 – 873Combined sources
    Beta strandi94 – 11219Combined sources
    Beta strandi125 – 13511Combined sources
    Beta strandi141 – 1455Combined sources
    Beta strandi148 – 1514Combined sources
    Beta strandi153 – 16917Combined sources
    Beta strandi180 – 1889Combined sources
    Beta strandi201 – 2077Combined sources
    Beta strandi213 – 2175Combined sources
    Turni219 – 2213Combined sources
    Beta strandi224 – 2296Combined sources
    Turni233 – 2353Combined sources
    Beta strandi241 – 2488Combined sources
    Turni250 – 2523Combined sources
    Beta strandi259 – 2624Combined sources
    Beta strandi271 – 2744Combined sources
    Beta strandi280 – 2834Combined sources
    Beta strandi285 – 2873Combined sources
    Beta strandi291 – 2955Combined sources
    Turni296 – 2994Combined sources
    Beta strandi300 – 3034Combined sources
    Beta strandi315 – 3184Combined sources
    Beta strandi324 – 3274Combined sources
    Beta strandi333 – 3353Combined sources
    Beta strandi340 – 3445Combined sources
    Turni345 – 3484Combined sources
    Beta strandi349 – 3535Combined sources
    Helixi359 – 3613Combined sources
    Helixi368 – 3703Combined sources
    Turni371 – 3733Combined sources
    Beta strandi378 – 3803Combined sources
    Helixi382 – 3843Combined sources
    Beta strandi386 – 3883Combined sources
    Beta strandi391 – 3999Combined sources
    Beta strandi405 – 4117Combined sources
    Beta strandi426 – 4316Combined sources
    Turni432 – 4354Combined sources
    Beta strandi436 – 4405Combined sources
    Beta strandi443 – 4508Combined sources
    Beta strandi455 – 4595Combined sources
    Beta strandi468 – 4714Combined sources
    Beta strandi480 – 4823Combined sources
    Beta strandi484 – 4874Combined sources
    Beta strandi493 – 4964Combined sources
    Beta strandi499 – 5013Combined sources
    Beta strandi515 – 5184Combined sources
    Helixi519 – 5213Combined sources
    Beta strandi523 – 5264Combined sources
    Beta strandi538 – 5425Combined sources
    Beta strandi548 – 5525Combined sources
    Beta strandi565 – 5706Combined sources
    Helixi572 – 5743Combined sources
    Beta strandi579 – 5813Combined sources
    Beta strandi587 – 5915Combined sources
    Beta strandi593 – 5964Combined sources
    Beta strandi600 – 6078Combined sources
    Beta strandi610 – 6167Combined sources
    Beta strandi619 – 6213Combined sources
    Beta strandi630 – 6323Combined sources
    Beta strandi635 – 6395Combined sources
    Beta strandi642 – 6465Combined sources
    Turni651 – 6533Combined sources
    Beta strandi656 – 6649Combined sources
    Beta strandi674 – 6796Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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. Positions 42-680.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini42 – 189148F5/8 type CPROSITE-ProRule annotationAdd
    BLAST
    Repeati223 – 26846Kelch 1Add
    BLAST
    Repeati279 – 32143Kelch 2Add
    BLAST
    Repeati323 – 37250Kelch 3Add
    BLAST
    Repeati436 – 49055Kelch 4Add
    BLAST
    Repeati492 – 54453Kelch 5Add
    BLAST

    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

    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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti111 – 1111M → I in AAB94635 (Ref. 4) Curated

    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
    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. Positions 42-680.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    CAZyiCBM32. 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

    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...

    Publicationsi

    1. "Galactose oxidase of Dactylium dendroides. Gene cloning and sequence analysis."
      McPherson M.J., Ogel Z.B., Stevens C.E., Yadav K.D.S., Keen J.N., Knowles P.F.
      J. Biol. Chem. 267:8146-8152(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: ATCC 46032 / CBS 110244 / NRRL 2903.
    2. "Galactose oxidase pro-sequence cleavage and cofactor assembly are self-processing reactions."
      Rogers M.S., Baron A.J., McPherson M.J., Knowles P.F., Dooley D.M.
      J. Am. Chem. Soc. 122:990-991(2000)
      Cited for: PROTEIN SEQUENCE OF 25-33 AND 42-50, PROPEPTIDE CLEAVAGE.
      Strain: ATCC 46032 / CBS 110244 / NRRL 2903.
    3. Cited for: PROTEIN SEQUENCE OF 42-47, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-371 AND PHE-505.
    4. "Specific identification of Fusarium graminearum by PCR with gaoA targeted primers."
      Niessen M.L., Vogel R.F.
      Syst. Appl. Microbiol. 20:111-123(1997)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 98-142.
      Strain: DSM 4527.
    5. "Galactose oxidase from Polyporus circinatus, Fr."
      Cooper J.A., Smith W., Bacila M., Medina H.
      J. Biol. Chem. 234:445-448(1959) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "The D-galactose oxidase of Polyporus circinatus."
      Avigad G., Amaral D., Asensio C., Horecker B.L.
      J. Biol. Chem. 237:2736-2743(1962) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBSTRATE SPECIFICITY.
    7. "Dactylium dendroides (Bull.) Fr. misnamed as Polyporus circinatus Fr."
      Nobles M.K., Madhosingh C.
      Biochem. Biophys. Res. Commun. 12:146-147(1963)
      Cited for: TAXONOMY.
    8. "Galactose oxidase of Polyporus circinatus: a copper enzyme."
      Amaral D., Bernstein L., Morse D., Horecker B.L.
      J. Biol. Chem. 238:2281-2284(1963) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, COPPER-BINDING.
    9. "The molecular properties of the copper enzyme galactose oxidase."
      Kosman D.J., Ettinger M.J., Weiner R.E., Massaro E.J.
      Arch. Biochem. Biophys. 165:456-467(1974) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    10. "Cellulose-triggered sporulation in the galactose oxidase producing fungus Cladobotryum (Dactylium) dendroides NRRL 2903 and its re-identification as a species of Fusarium."
      Ogel Z.B., Brayford D., McPherson M.J.
      Mycol. Res. 98:474-480(1994)
      [AGRICOLA] [Europe PMC]
      Cited for: TAXONOMY.
    11. "Catalytic reaction profile for alcohol oxidation by galactose oxidase."
      Whittaker M.M., Whittaker J.W.
      Biochemistry 40:7140-7148(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: REACTION MECHANISM.
    12. "Cu(I)-dependent biogenesis of the galactose oxidase redox cofactor."
      Whittaker M.M., Whittaker J.W.
      J. Biol. Chem. 278:22090-22101(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN MATURATION.
    13. "Novel thioether bond revealed by a 1.7 A crystal structure of galactose oxidase."
      Ito N., Phillips S.E.V., Stevens C.E., Ogel Z.B., McPherson M.J., Keen J.N., Yadav K.D.S., Knowles P.F.
      Nature 350:87-90(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 42-680 IN COMPLEX WITH COPPER IONS.
    14. "Structure and mechanism of galactose oxidase. The free radical site."
      Baron A.J., Stevens C., Wilmot C., Seneviratne K.D., Blakeley V., Dooley D.M., Phillips S.E., Knowles P.F., McPherson M.J.
      J. Biol. Chem. 269:25095-25105(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 42-680 OF MUTANTS GLY-269 AND HIS-331 IN COMPLEX WITH COPPER IONS, BIOPHYSICOCHEMICAL PROPERTIES.
    15. "Structure and mechanism of galactose oxidase: catalytic role of tyrosine 495."
      Reynolds M.P., Baron A.J., Wilmot C.M., Vinecombe E., Stevens C., Phillips S.E.V., Knowles P.F., McPherson M.J.
      J. Biol. Inorg. Chem. 2:327-335(1997)
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 42-680 OF MUTANT PHE-536 IN COMPLEX WITH COPPER IONS, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES.
    16. "Crystal structure of the precursor of galactose oxidase: an unusual self-processing enzyme."
      Firbank S.J., Rogers M.S., Wilmot C.M., Dooley D.M., Halcrow M.A., Knowles P.F., McPherson M.J., Phillips S.E.
      Proc. Natl. Acad. Sci. U.S.A. 98:12932-12937(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 25-680.
    17. "Structural and kinetic studies of a series of mutants of galactose oxidase identified by directed evolution."
      Wilkinson D., Akumanyi N., Hurtado-Guerrero R., Dawkes H., Knowles P.F., Phillips S.E.V., McPherson M.J.
      Protein Eng. Des. Sel. 17:141-148(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 42-680 OF MUTANT SER-424 IN COMPLEX WITH COPPER IONS, MASS SPECTROMETRY, MUTAGENESIS OF CYS-424; TYR-477 AND VAL-535, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: ATCC 46032 / CBS 110244 / NRRL 2903.
    18. "The stacking tryptophan of galactose oxidase: a second-coordination sphere residue that has profound effects on tyrosyl radical behavior and enzyme catalysis."
      Rogers M.S., Tyler E.M., Akyumani N., Kurtis C.R., Spooner R.K., Deacon S.E., Tamber S., Firbank S.J., Mahmoud K., Knowles P.F., Phillips S.E.V., McPherson M.J., Dooley D.M.
      Biochemistry 46:4606-4618(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 42-680 OF MUTANTS GLY-331; HIS-331 AND PHE-331 IN COMPLEX WITH COPPER IONS, BIOPHYSICOCHEMICAL PROPERTIES.

    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 11, 2015
    This is version 20 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.