P48842 (GANA_ASPAC) Reviewed, UniProtKB/Swiss-Prot

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

Gene names

Name:

gal1

Organism

Aspergillus aculeatus

Taxonomic identifier

5053 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	350 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)

Catalytic activity	The enzyme specifically hydrolyzes (1->4)-beta-D-galactosidic linkages in type I arabinogalactans.
Post-translational modification	Glycosylated.
Sequence similarities	Belongs to the glycosyl hydrolase 53 family.
Biophysicochemical properties	pH dependence: Optimum pH is 4.0-4.5. Temperature dependence: Optimum temperature is 40-65 degrees Celsius.

Ontologies

Keywords
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	arabinogalactan endo-1,4-beta-galactosidase activity Inferred from electronic annotation. Source: EC glucosidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 16

16

Ref.1

Chain

17 – 350

334

Arabinogalactan endo-1,4-beta-galactosidase

PRO_0000012221

Sites

Active site

152

1

Proton donor By similarity

Active site

262

1

Nucleophile By similarity

Amino acid modifications

Glycosylation

128

1

N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis

198

1

D → N: Broadens pH profile by 1 unit towards the basic end of the scale. Ref.2

Secondary structure

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350

Helix Strand Turn

Details...

Beta strand

19 – 24

6

Helix

28 – 33

6

Helix

48 – 55

8

Beta strand

59 – 64

6

Helix

75 – 87

13

Beta strand

91 – 96

6

Beta strand

99 – 101

3

Helix

119 – 139

21

Beta strand

145 – 152

8

Helix

153 – 155

3

Beta strand

157 – 159

3

Turn

160 – 162

3

Helix

167 – 182

16

Beta strand

191 – 197

7

Helix

202 – 214

13

Beta strand

216 – 218

3

Helix

220 – 222

3

Beta strand

225 – 229

5

Beta strand

232 – 234

3

Helix

240 – 254

15

Beta strand

258 – 262

5

Helix

278 – 280

3

Helix

287 – 302

16

Beta strand

307 – 313

7

Turn

321 – 324

4

Beta strand

325 – 329

5

Turn

335 – 337

3

Helix

343 – 348

6

Sequences

	Sequence		Length	Mass (Da)
	P48842 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 9074249DFAB24CAC	FASTA	350	38,423
	10 20 30 40 50 60 MFASLLLAAL PLLTHAALTY RGADISSLLL LEDEGYSYKN LNGQTQALET ILADAGINSI 70 80 90 100 110 120 RQRVWVNPSD GSYDLDYNLE LAKRVKAAGM SLYLDLHLSD TWADPSDQTT PSGWSTTDLG 130 140 150 160 170 180 TLKWQLYNYT LEVCNTFAEN DIDIEIISIG NEIRAGLLWP LGETSSYSNI GALLHSGAWG 190 200 210 220 230 240 VKDSNLATTP KIMIHLDDGW SWDQQNYFYE TVLATGELLS TDFDYFGVSY YPFYSASATL 250 260 270 280 290 300 ASLKTSLANL QSTYDKPVVV VETNWPVSCP NPAYAFPSDL SSIPFSVAGQ QEFLEKLAAV 310 320 330 340 350 VEATTDGLGV YYWEPAWIGN AGLGSSCADN LMVDYTTDEV YESIETLGEL

References

[1]	"Expression cloning, purification and characterization of a beta-1,4-galactanase from Aspergillus aculeatus." Christgau S., Sandal T., Kofod L.V., Dalboege H. Curr. Genet. 27:135-141(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-44. Strain: KSM 510.
[2]	"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] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ASP-198.
[3]	"Aspergillus aculeatus beta-1,4-galactanase: substrate recognition and relations to other glycoside hydrolases in clan GH-A." Ryttersgaard C., Lo Leggio L., Coutinho P.M., Henrissat B., Larsen S. Biochemistry 41:15135-15143(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L34599 mRNA. Translation: AAA32692.1.

PIR

S51494.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FHL	X-ray	2.30	A	17-350	[»]
1FOB	X-ray	1.80	A	17-350	[»]

ProteinModelPortal

P48842.

SMR

P48842. Positions 17-350.

ModBase

Search...

Protein family/group databases

CAZy

GH53. Glycoside Hydrolase Family 53.

mycoCLAP

GAN53A_ASPAC.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

3.20.20.80. 1 hit.

InterPro

IPR011683. Glyco_hydro_53.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Pfam

PF07745. Glyco_hydro_53. 1 hit.
[Graphical view]

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P48842.

Entry information

Entry name

GANA_ASPAC

Accession

Primary (citable) accession number: P48842

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program