Q03045 (AMYG_HORRE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glucoamylase P
EC=3.2.1.3

Alternative name(s):
1,4-alpha-D-glucan glucohydrolase
Glucan 1,4-alpha-glucosidase

Gene names

Name:

GAMP

Organism

Hormoconis resinae (Creosote fungus) (Amorphotheca resinae)

Taxonomic identifier

5101 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Leotiomycetes › Leotiomycetes incertae sedis › Myxotrichaceae › Amorphotheca

Protein attributes

Sequence length	616 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	Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose.
Subcellular location	Secreted.
Sequence similarities	Belongs to the glycosyl hydrolase 15 family. Contains 1 CBM20 (carbohydrate binding type-20) domain.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Polysaccharide degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	glucan 1,4-alpha-glucosidase activity Inferred from electronic annotation. Source: EC starch binding 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 – 29	29
	Chain	30 – 616	587	Glucoamylase P		PRO_0000001471
Regions
	Domain	501 – 608	108	CBM20
Sites
	Active site	205	1	Proton acceptor By similarity
	Active site	208	1	Proton donor By similarity
	Binding site	149	1	Substrate By similarity
Amino acid modifications
	Glycosylation	200	1	N-linked (GlcNAc...) Potential
	Glycosylation	427	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q03045 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: B5F4DC8EEBB152FB	FASTA	616	66,432
	10 20 30 40 50 60 MRLLPSSCAG ALSLLCSLAI AAPTELKARD LSSFIASERA IALQGALNNI GPDGSAVPGA 70 80 90 100 110 120 GAGFVVASPS KANPDYFYTW SRDSALTLKM IIDEFILGNT TLQTIIEQYI HAQAVLQTVS 130 140 150 160 170 180 NPSGTFLPDG VGLGEPKFMV DGTRFNGPWG RPQRDGPALR AIALMTYSNW LIKNGQFAEA 190 200 210 220 230 240 KTKIWPIIAN DLSYVGQYWN QSGFDLWEET YASSFFTIQN QHRALVEGAQ LAHDLGVTCT 250 260 270 280 290 300 GCDQAPEVLC FLQSFWNGKY IVSNINVNNG RTGLDGNSIL GAISTFDIDA YCDSPTLQPC 310 320 330 340 350 360 HSQSLANFKV LTDTFRNLYT INAGIPEGQG VAVGRYAEDV YMGGNPWYLI TTAAAEFLYD 370 380 390 400 410 420 AVAQWKARHV LTVDETSLAF FKDIYPEVTV REYKSGNANS PFAQIMDAVT AYADSYVAIA 430 440 450 460 470 480 EKYIPSNGSL SEQFNRDTGT PLSAIDLTWS YAAFITMSQR RAGQYPSSWG SRNALPPPTT 490 500 510 520 530 540 CSASSTPGIY TPATAAGAPN VTSSCQVSIT FNINATTYYG ENLYVIGNSS DLGAWNIADA 550 560 570 580 590 600 YPLSASAYTQ DRPLWSAAIP LNAGEVISYQ YVRQEDCDQP YIYETVNRTL TVPACGGAAV 610 TTDDAWMGPV GSSGNC

References

[1]	"Glucoamylase P gene of Hormoconis resinae: molecular cloning, sequencing and introduction into Trichoderma reesei." Joutsjoki V.V., Torkkeli T.K. FEMS Microbiol. Lett. 78:237-243(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 20495 / CBS 174.61 / NRRL 6437.
[2]	"Cloning and expression of Hormoconis resinae glucoamylase P cDNA in Saccharomyces cerevisiae." Vainio A.E.I., Torkkeli H.T., Tuusa T., Aho S.A., Fagerstroem B.R., Korhola M.P. Curr. Genet. 24:38-44(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: ATCC 20495 / CBS 174.61 / NRRL 6437.
[3]	"Comparison of two glucoamylases from Hormoconis resinae." Fagerstroem R., Vainio A.E.I., Suoranta K., Pakula T., Kalkkinen N., Torkkeli H.T. J. Gen. Microbiol. 136:913-920(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 72-76, CHARACTERIZATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X68143 Genomic DNA. Translation: CAA48243.1. X67708 mRNA. Translation: CAA47945.1.
PIR	S33908.
3D structure databases
ProteinModelPortal	Q03045.
SMR	Q03045. Positions 30-503.
ModBase	Search...
Protein family/group databases
CAZy	CBM20. Carbohydrate-Binding Module Family 20. GH15. Glycoside Hydrolase Family 15.
mycoCLAP	GLA15P_HORRE.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	1.50.10.10. 1 hit. 2.60.40.10. 1 hit.
InterPro	IPR008928. 6-hairpin_glycosidase-like. IPR012341. 6hp_glycosidase. IPR013784. Carb-bd-like_fold. IPR002044. CBM_fam20. IPR000165. Glucoamylase. IPR008291. Glucoamylase_SBD. IPR011613. Glyco_hydro_15. IPR013783. Ig-like_fold. [Graphical view]
Pfam	PF00686. CBM_20. 1 hit. PF00723. Glyco_hydro_15. 1 hit. [Graphical view]
PIRSF	PIRSF001031. Glu-a-glcsd_SBD. 1 hit.
PRINTS	PR00736. GLHYDRLASE15.
SMART	SM01065. CBM_2. 1 hit. [Graphical view]
SUPFAM	SSF49452. CBD_4. 1 hit. SSF48208. Glyco_trans_6hp. 1 hit.
PROSITE	PS51166. CBM20. 1 hit. PS00820. GLUCOAMYLASE. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMYG_HORRE

Accession

Primary (citable) accession number: Q03045

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	April 3, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program