GAOA_GIBZE
ID GAOA_GIBZE Reviewed; 680 AA.
AC I1S2N3; A0A098DZ82; A0A0E0SL48; O43098; Q01745; Q4HVH6; V6RUL9;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Galactose oxidase;
DE Short=GAO;
DE Short=GO;
DE Short=GOase;
DE EC=1.1.3.9;
DE Flags: Precursor;
GN Name=GAOA; ORFNames=FGRRES_11032, FGSG_11032;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
CC -!- FUNCTION: Catalyzes the sterospecific oxidation of primary alcohols to
CC the corresponding aldehydes. The biologically relevant substrate of the
CC enzyme is not known as the enzyme exhibits broad substrate specificity
CC from small alcohols through sugars to oligo- and polysaccharides (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactose + O2 = D-galacto-hexodialdose + H2O2;
CC Xref=Rhea:RHEA:24160, ChEBI:CHEBI:4139, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16222, ChEBI:CHEBI:16240; EC=1.1.3.9;
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250};
CC Note=Binds 1 Cu(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- PTM: Galactose oxidase contains a protein-derived free radical cofactor
CC (By similarity). In the active state, Tyr-313, which is cross-linked to
CC Cys-269 via a thioether bond, is oxidized to a radical and acts with
CC Cu(2+) as a two-electron acceptor in the oxidation reaction. The cross-
CC link is believed to modulate the redox potential of the tyrosyl
CC radical, which is further stabilized by a stacking interaction with
CC Trp-331 in the active site. The post-translational formation of the
CC cross-link is closely linked to the propeptide cleavage event, and both
CC are copper-dependent, autocatalytic processes. The propeptide may act
CC as an intramolecular chaperone, facilitating thioester bond formation
CC and copper binding by positioning of active-site residues, including
CC copper ligands (By similarity). {ECO:0000250}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/GAO/";
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DR EMBL; DS231670; ESU17707.1; -; Genomic_DNA.
DR EMBL; HG970334; CEF87161.1; -; Genomic_DNA.
DR RefSeq; XP_011325329.1; XM_011327027.1.
DR AlphaFoldDB; I1S2N3; -.
DR SMR; I1S2N3; -.
DR STRING; 5518.FGSG_11032P0; -.
DR EnsemblFungi; ESU17707; ESU17707; FGSG_11032.
DR GeneID; 23557903; -.
DR KEGG; fgr:FGSG_11032; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G21069; -.
DR eggNOG; ENOG502SCD5; Eukaryota.
DR HOGENOM; CLU_013444_1_1_1; -.
DR InParanoid; I1S2N3; -.
DR Proteomes; UP000070720; Chromosome 3.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0045480; F:galactose oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd02851; E_set_GO_C; 1.
DR CDD; cd00057; FA58C; 1.
DR Gene3D; 2.130.10.80; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR037293; Gal_Oxidase_central_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR015202; GO-like_E_set.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR006652; Kelch_1.
DR Pfam; PF09118; DUF1929; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF01344; Kelch_1; 1.
DR SMART; SM00231; FA58C; 1.
DR SMART; SM00612; Kelch; 3.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF50965; SSF50965; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50022; FA58C_3; 1.
PE 3: Inferred from homology;
KW Copper; Disulfide bond; Kelch repeat; Metal-binding; Oxidoreductase;
KW Reference proteome; Repeat; Secreted; Signal; Thioether bond.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT PROPEP 25..41
FT /evidence="ECO:0000250"
FT /id="PRO_0000418370"
FT CHAIN 42..680
FT /note="Galactose oxidase"
FT /id="PRO_0000418371"
FT DOMAIN 42..189
FT /note="F5/8 type C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT REPEAT 223..268
FT /note="Kelch 1"
FT REPEAT 279..321
FT /note="Kelch 2"
FT REPEAT 323..372
FT /note="Kelch 3"
FT REPEAT 436..490
FT /note="Kelch 4"
FT REPEAT 492..544
FT /note="Kelch 5"
FT ACT_SITE 536
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 313
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 536
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 537
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 622
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT DISULFID 59..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DISULFID 556..559
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT CROSSLNK 269..313
FT /note="3'-(S-cysteinyl)-tyrosine (Cys-Tyr)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 680 AA; 72791 MW; 7883D8F9637E8FE9 CRC64;
MKHFLSLALC FSSINAVAVT VPHKSGGTGS PEGSLQFLSL RASAPIGSAI SRNNWAVTCD
SAQSGNECNK AIDGNKDTFW HTFYGANGDP KPPHTYTIDM KTTQNVNGLS MLPRQDGNQN
GWIGRHEVYL SSDGTNWGSP VASGSWFADS TTKYSNFETR PARYVRLVAV TEANGQPWTS
IAEINVFQAS SYTAPQPGLG RWGPTIDLPI VPAAAAIEPT SGRVLMWSSY RNDAFGGSPG
GITLTSSWDP STGIVSDRTV TVTKHDMFCP GISMDGNGQI VVTGGNDAKK TSLYDSSSDS
WIPGPDMQVA RGYQSSATMS DGRVFTIGGS WSGGVFEKNG EVYSPSSKTW TSLPNAKVNP
MLTADKQGLY RSDNHAWLFG WKKGSVFQAG PSTAMNWYYT SGSGDVKSAG KRQSNRGVAP
DAMCGNAVMY DAVKGKILTF GGSPDYQDSD ATTNAHIITL GEPGTSPNTV FASNGLYFAR
TFHTSVVLPD GSTFITGGQR RGIPFEDSTP VFTPEIYVPE QDTFYKQNPN SIVRVYHSIS
LLLPDGRVFN GGGGLCGDCT TNHFDAQIFT PNYLYNSNGN LATRPKITRT STQSVKVGGR
ITISTDSSIT KASLIRYGTA THTVNTDQRR IPLTLTNNGG NSYSFQVPSD SGVALPGYWM
LFVMNSAGVP SVASTIRVTQ
