Reviewed, UniProtKB/Swiss-Prot P83692 (GANA_THIHE)

Names and origin

Protein names	Recommended name:     Arabinogalactan endo-1,4-beta-galactosidase     EC=3.2.1.89 Alternative name(s):     Endo-1,4-beta-galactanase       Short name=Galactanase
Organism	Thielavia heterothallica (Myceliophthora thermophila)
Taxonomic identifier	78579 [NCBI]
Taxonomic lineage	Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Chaetomiaceae › Thielavia

Protein attributes

Sequence length	332 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Endohydrolysis of (1->4)-beta-D-galactosidic linkages in arabinogalactans. Ref.1
Miscellaneous	Has a pH range of 5.5-8.5 with optimum of 7.0; and a temperature optimum of 65 degrees Celsius at pH 6.5. Ref.1
Sequence similarities	Belongs to the glycosyl hydrolase 53 family. Ref.1

Ontologies

Keywords
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro cell wall macromolecule catabolic process Ref.1 Traceable author statement. Source: UniProtKB
Cellular component	extraorganismal space Ref.1 Inferred by curator. Source: UniProtKB
Molecular function	arabinogalactan endo-1,4-beta-galactosidase activity Inferred from electronic annotation. Source: EC cation binding Inferred from electronic annotation. Source: InterPro glucosidase activity Inferred from electronic annotation. Source: InterPro polysaccharide binding Ref.1 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 332

332

Arabinogalactan endo-1,4-beta-galactosidase

PRO_0000057706

Sites

Active site

135

1

Proton donor By similarity UniProtKB P48841

Active site

245

1

Nucleophile By similarity UniProtKB P48841

Amino acid modifications

Glycosylation

111

1

N-linked (GlcNAc...) Ref.1

Experimental info

Mutagenesis

90 – 91

2

AH → SD: Lowers pH profile by 0.5 units. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

332

Helix Strand Turn

Details...

Beta strand

3 – 8

6

Helix

12 – 17

6

Helix

32 – 38

7

Beta strand

43 – 48

6

Helix

59 – 71

13

Beta strand

75 – 80

6

Beta strand

83 – 85

3

Helix

102 – 122

21

Beta strand

128 – 135

8

Helix

136 – 138

3

Helix

150 – 165

16

Beta strand

174 – 180

7

Helix

185 – 196

12

Beta strand

199 – 201

3

Helix

203 – 205

3

Beta strand

208 – 212

5

Beta strand

215 – 217

3

Helix

223 – 237

15

Beta strand

240 – 245

6

Helix

261 – 263

3

Helix

270 – 285

16

Beta strand

290 – 296

7

Helix

301 – 303

3

Turn

304 – 307

4

Beta strand

308 – 312

5

Beta strand

320 – 322

3

Helix

324 – 330

7

Sequences

	Sequence		Length	Mass (Da)
	P83692-1 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: 71CA092FDB1D43DC	FASTA	332	36,812
	10 20 30 40 50 60 ALTYRGVDWS SVVVEERAGV SYKNTNGNAQ PLENILAANG VNTVRQRVWV NPADGNYNLD 70 80 90 100 110 120 YNIAIAKRAK AAGLGVYIDF HYSDTWADPA HQTMPAGWPS DIDNLSWKLY NYTLDAANKL 130 140 150 160 170 180 QNAGIQPTIV SIGNEIRAGL LWPTGRTENW ANIARLLHSA AWGIKDSSLS PKPKIMIHLD 190 200 210 220 230 240 NGWDWGTQNW WYTNVLKQGT LELSDFDMMG VSFYPFYSSS ATLSALKSSL DNMAKTWNKE 250 260 270 280 290 300 IAVVETNWPI SCPNPRYSFP SDVKNIPFSP EGQTTFITNV ANIVSSVSRG VGLFYWEPAW 310 320 330 IHNANLGSSC ADNTMFSQSG QALSSLSVFQ RI

References

[1]

"Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum." Le Nours J., Ryttersgaard C., Lo Leggio L., Oestergaard P.R., Borchert T.V., Christensen L.L.H., Larsen S. Protein Sci. 12:1195-1204(2003) [PubMed: 12761390] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), CATALYTIC ACTIVITY, GLYCOSYLATION AT ASN-111, MUTAGENESIS OF 90-ASP-HIS-91.

Cross-references

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HJS	X-ray	1.87	A/B/C/D	1-332	[»]
1HJU	X-ray	2.15	A/B/C/D	1-332	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH53. Glycoside Hydrolase Family 53.

Enzyme and pathway databases

BRENDA

3.2.1.89. 280423.

Family and domain databases

InterPro

IPR011683. Glyco_hydro_53.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

Pfam

PF07745. Glyco_hydro_53. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GANA_THIHE

Accession

Primary (citable) accession number: P83692

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 7, 2004
Last sequence update:	December 15, 2003
Last modified:	June 16, 2009
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)