Q01745 (GAOA_GIBZE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Galactose oxidase
Short name=GAO
Short name=GO
Short name=GOase
EC=1.1.3.9

Gene names

Name:	GAOA
ORF Names:	FG11032

Organism

Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084) (Wheat head blight fungus) (Fusarium graminearum)

Taxonomic identifier

229533 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › Nectriaceae › Gibberella

Protein attributes

Sequence length	680 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.6 Ref.10
Catalytic activity	D-galactose + O2 = D-galacto-hexodialdose + H2O2.
Cofactor	Binds 1 Cu2+ ion per subunit.
Enzyme regulation	Inhibited by diethyldithiocarbamate. Ref.9
Subunit structure	Monomer. Ref.10
Subcellular location	Secreted.
Post-translational modification	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.
Sequence similarities	Contains 1 F5/8 type C domain. Contains 3 Kelch repeats.
Caution	Was originally thought to originate from Polyporus circinatus then later from Dactylium dendroides and is now known to be originating from Gibberella (Fusarium).
Biophysicochemical properties	Kinetic parameters: KM=56 mM for 1-methyl-alpha-D-galactopyranoside Ref.4 Ref.15 Ref.16 Ref.18 Ref.19 KM=57 mM for 2-methylene-1,3-propanediol KM=68 mM for D-galactose KM=2.5 M for D-fructose pH dependence: Optimum pH is 7. Active from pH 5.7 to 9.4.
Mass spectrometry	Molecular mass is 68520 Da from positions 42 - 680. Determined by ESI. Ref.18
Sequence caution	The sequence EAA74855.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Secreted
Domain	Kelch repeat Repeat Signal
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond Thioether bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cell adhesion Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	galactose oxidase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

Ref.3

Propeptide

25 – 41

17

PRO_0000285407

Chain

42 – 680

639

Galactose oxidase

PRO_0000016610

Regions

Domain

42 – 189

148

F5/8 type C

Repeat

279 – 321

43

Kelch 1

Repeat

323 – 372

50

Kelch 2

Repeat

492 – 544

53

Kelch 3

Sites

Active site

536

1

Proton acceptor Ref.16

Metal binding

313

1

Copper

Metal binding

536

1

Copper

Metal binding

537

1

Copper

Metal binding

622

1

Copper

Amino acid modifications

Disulfide bond

59 ↔ 68

Disulfide bond

556 ↔ 559

Cross-link

269 ↔ 313

3'-(S-cysteinyl)-tyrosine (Cys-Tyr)

Natural variations

Natural variant

4 – 6

3

LLT → FLS in strain: PH-1 / NRRL 31084.

Natural variant

25 – 26

2

AV → SG in strain: PH-1 / NRRL 31084.

Natural variant

30

1

I → S in strain: PH-1 / NRRL 31084.

Natural variant

170

1

I → V in strain: PH-1 / NRRL 31084.

Natural variant

610

1

S → T in strain: PH-1 / NRRL 31084.

Experimental info

Mutagenesis

269

1

C → G: Reduces catalytic activity more than 10000-fold.

Mutagenesis

331

1

W → F: Reduces catalytic efficiency 50-fold and substrate affinity 36-fold.

Mutagenesis

331

1

W → G: Reduces substrate affinity 20-fold and catalytic activity more than 6000-fold.

Mutagenesis

331

1

W → H: Reduces catalytic efficiency 1000-fold.

Mutagenesis

371

1

R → A: Reduces catalytic efficiency 250-fold and substrate affinity 22-fold for D-galactose, but improves catalytic efficieny 1.8-fold towards D-fructose. Ref.4

Mutagenesis

371

1

R → K: Reduces catalytic efficiency 45-fold and substrate affinity 8.7-fold for D-galactose, but improves catalytic efficieny 8-fold towards D-fructose. Ref.4

Mutagenesis

424

1

C → A: Reduces catalytic efficiency 1.5-to 2-fold towards D-galactose and 1-methyl-alpha-D-galactopyranoside. Ref.18

Mutagenesis

424

1

C → 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. Ref.18

Mutagenesis

477

1

Y → 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. Ref.18

Mutagenesis

477

1

Y → H: No effect. Improves catalytic efficiency 5.3-fold towards D-galactose; when associated with S-424. Ref.18

Mutagenesis

505

1

F → A: Reduces catalytic efficiency 166-fold and substrate affinity 9-fold. Ref.4

Mutagenesis

535

1

V → 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. Ref.18

Mutagenesis

536

1

Y → F: Reduces catalytic efficiency 1000-fold, but does not reduce substrate affinity.

Sequence conflict

111

1

M → I in AAB94635. Ref.5

Secondary structure

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680

Helix Strand Turn

Details...

Helix

35 – 37

3

Beta strand

46 – 49

4

Beta strand

56 – 60

5

Helix

68 – 71

4

Beta strand

72 – 74

3

Helix

85 – 87

3

Beta strand

94 – 112

19

Beta strand

125 – 135

11

Beta strand

141 – 145

5

Beta strand

148 – 151

4

Beta strand

153 – 169

17

Beta strand

180 – 188

9

Beta strand

201 – 207

7

Beta strand

213 – 217

5

Turn

219 – 221

3

Beta strand

224 – 229

6

Turn

233 – 235

3

Beta strand

241 – 248

8

Turn

250 – 252

3

Beta strand

259 – 262

4

Beta strand

271 – 274

4

Beta strand

280 – 283

4

Beta strand

285 – 287

3

Beta strand

291 – 295

5

Turn

296 – 299

4

Beta strand

300 – 303

4

Beta strand

315 – 318

4

Beta strand

324 – 327

4

Beta strand

333 – 335

3

Beta strand

340 – 344

5

Turn

345 – 348

4

Beta strand

349 – 353

5

Helix

359 – 361

3

Helix

368 – 370

3

Turn

371 – 373

3

Beta strand

378 – 380

3

Helix

382 – 384

3

Beta strand

386 – 388

3

Beta strand

391 – 399

9

Beta strand

405 – 411

7

Beta strand

426 – 431

6

Turn

432 – 435

4

Beta strand

436 – 440

5

Beta strand

443 – 450

8

Beta strand

455 – 459

5

Beta strand

468 – 471

4

Beta strand

484 – 487

4

Beta strand

493 – 496

4

Beta strand

499 – 501

3

Beta strand

515 – 518

4

Helix

519 – 521

3

Beta strand

523 – 526

4

Beta strand

538 – 542

5

Beta strand

548 – 552

5

Beta strand

565 – 570

6

Helix

572 – 574

3

Beta strand

579 – 581

3

Beta strand

587 – 591

5

Beta strand

593 – 596

4

Beta strand

600 – 607

8

Beta strand

610 – 616

7

Beta strand

619 – 621

3

Beta strand

630 – 632

3

Beta strand

635 – 639

5

Beta strand

642 – 646

5

Turn

651 – 653

3

Beta strand

656 – 664

9

Beta strand

674 – 679

6

Sequences

	Sequence		Length	Mass (Da)
	Q01745 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 2F97C561B63E46E9	FASTA	680	72,823
	10 20 30 40 50 60 MKHLLTLALC FSSINAVAVT VPHKAVGTGI PEGSLQFLSL RASAPIGSAI SRNNWAVTCD 70 80 90 100 110 120 SAQSGNECNK AIDGNKDTFW HTFYGANGDP KPPHTYTIDM KTTQNVNGLS MLPRQDGNQN 130 140 150 160 170 180 GWIGRHEVYL SSDGTNWGSP VASGSWFADS TTKYSNFETR PARYVRLVAI TEANGQPWTS 190 200 210 220 230 240 IAEINVFQAS SYTAPQPGLG RWGPTIDLPI VPAAAAIEPT SGRVLMWSSY RNDAFGGSPG 250 260 270 280 290 300 GITLTSSWDP STGIVSDRTV TVTKHDMFCP GISMDGNGQI VVTGGNDAKK TSLYDSSSDS 310 320 330 340 350 360 WIPGPDMQVA RGYQSSATMS DGRVFTIGGS WSGGVFEKNG EVYSPSSKTW TSLPNAKVNP 370 380 390 400 410 420 MLTADKQGLY RSDNHAWLFG WKKGSVFQAG PSTAMNWYYT SGSGDVKSAG KRQSNRGVAP 430 440 450 460 470 480 DAMCGNAVMY DAVKGKILTF GGSPDYQDSD ATTNAHIITL GEPGTSPNTV FASNGLYFAR 490 500 510 520 530 540 TFHTSVVLPD GSTFITGGQR RGIPFEDSTP VFTPEIYVPE QDTFYKQNPN SIVRVYHSIS 550 560 570 580 590 600 LLLPDGRVFN GGGGLCGDCT TNHFDAQIFT PNYLYNSNGN LATRPKITRT STQSVKVGGR 610 620 630 640 650 660 ITISTDSSIS KASLIRYGTA THTVNTDQRR IPLTLTNNGG NSYSFQVPSD SGVALPGYWM 670 680 LFVMNSAGVP SVASTIRVTQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 1569070] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: ATCC 46032 / CBS 110244 / NRRL 2903.
[2]	"The Fusarium graminearum genome reveals a link between localized polymorphism and pathogen specialization." Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A., Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T., Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S. , Goswami R.S., Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S., Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R., Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T., Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M., Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C. Science 317:1400-1402(2007) [PubMed: 17823352] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084.
[3]	"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.
[4]	"Enhanced fructose oxidase activity in a galactose oxidase variant." Deacon S.E., Mahmoud K., Spooner R.K., Firbank S.J., Knowles P.F., Phillips S.E., McPherson M.J. ChemBioChem 5:972-979(2004) [PubMed: 15239055] [Abstract] Cited for: PROTEIN SEQUENCE OF 42-47, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-371 AND PHE-505.
[5]	"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.
[6]	"Galactose oxidase from Polyporus circinatus, Fr." Cooper J.A., Smith W., Bacila M., Medina H. J. Biol. Chem. 234:445-448(1959) [PubMed: 13641238] [Abstract] Cited for: FUNCTION.
[7]	"The D-galactose oxidase of Polyporus circinatus." Avigad G., Amaral D., Asensio C., Horecker B.L. J. Biol. Chem. 237:2736-2743(1962) [PubMed: 13863403] [Abstract] Cited for: SUBSTRATE SPECIFICITY.
[8]	"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.
[9]	"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: 14012475] [Abstract] Cited for: ENZYME REGULATION, COPPER-BINDING.
[10]	"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: 4441089] [Abstract] Cited for: FUNCTION, SUBUNIT.
[11]	"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: IND20498749] Cited for: TAXONOMY.
[12]	"Catalytic reaction profile for alcohol oxidation by galactose oxidase." Whittaker M.M., Whittaker J.W. Biochemistry 40:7140-7148(2001) [PubMed: 11401560] [Abstract] Cited for: REACTION MECHANISM.
[13]	"Cu(I)-dependent biogenesis of the galactose oxidase redox cofactor." Whittaker M.M., Whittaker J.W. J. Biol. Chem. 278:22090-22101(2003) [PubMed: 12672814] [Abstract] Cited for: PROTEIN MATURATION.
[14]	"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: 2002850] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 42-680 IN COMPLEX WITH COPPER IONS.
[15]	"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: 7929198] [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.
[16]	"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.
[17]	"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: 11698678] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 25-680.
[18]	"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: 15047910] [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.
[19]	"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: 17385891] [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.
+	Additional computationally mapped references.

Web resources

Worthington enzyme manual

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M86819 Unassigned DNA. Translation: AAA16228.1.
AACM01000458 Genomic DNA. Translation: EAA74855.1. Different initiation.
U51094 Genomic DNA. Translation: AAB94635.1.

RefSeq

XP_391208.1. XM_391208.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GOF	X-ray	1.70	A	42-680	[»]
1GOG	X-ray	1.90	A	42-680	[»]
1GOH	X-ray	2.20	A	42-680	[»]
1K3I	X-ray	1.40	A	25-680	[»]
1T2X	X-ray	2.30	A	42-680	[»]
2EIB	X-ray	2.10	A	42-680	[»]
2EIC	X-ray	2.80	A	42-680	[»]
2EID	X-ray	2.20	A	42-680	[»]
2EIE	X-ray	1.80	A	42-680	[»]
2JKX	X-ray	1.84	A	42-680	[»]
2VZ1	X-ray	1.91	A	42-680	[»]
2VZ3	X-ray	1.90	A	42-680	[»]
2WQ8	X-ray	2.19	A	42-680	[»]

ProteinModelPortal

Q01745.

SMR

Q01745. Positions 42-680.

ModBase

Search...

Protein family/group databases

CAZy

CBM32. Carbohydrate-Binding Module Family 32.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

2792888.

KEGG

fgr:FG11032.1.

Phylogenomic databases

eggNOG

fuNOG08393.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-15357.

Family and domain databases

InterPro

IPR000421. Coagulation_fac_5/8-C_type_dom.
IPR015202. DUF1929.
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]

Gene3D

G3DSA:2.130.10.80. Gal_Oxidase_b-propeller. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 1 hit.

KO

K04618.

Pfam

PF09118. DUF1929. 1 hit.
PF00754. F5_F8_type_C. 1 hit.
PF01344. Kelch_1. 1 hit.
[Graphical view]

SMART

SM00231. FA58C. 1 hit.
SM00612. Kelch. 3 hits.
[Graphical view]

SUPFAM

SSF49785. Gal_bind_like. 1 hit.
SSF50965. Gal_oxid_central. 1 hit.
SSF81296. Ig_E-set. 1 hit.

PROSITE

PS50022. FA58C_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GAOA_GIBZE

Accession

Primary (citable) accession number: Q01745
Secondary accession number(s): O43098, Q4HVH6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	November 16, 2011
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program