Glucoamylase 1 precursor - Debaryomyces occidentalis (Yeast)

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Reviewed, UniProtKB/Swiss-Prot P22861 (AMYG_DEBOC)

Last modified April 14, 2009. Version 44. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names

Recommended name:
    Glucoamylase 1
    EC=3.2.1.3
Alternative name(s):
    Glucan 1,4-alpha-glucosidase
    1,4-alpha-D-glucan glucohydrolase

Gene names

Name:

GAM1

Organism

Debaryomyces occidentalis (Yeast) (Schwanniomyces occidentalis)

Taxonomic identifier

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Debaryomyces

Protein attributes

Sequence length	958 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

This glucoamylase has a specificity toward both alpha-1,4 and alpha-1,6 linkages.

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.

Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose.

Sequence similarities

Belongs to the glycosyl hydrolase 31 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Polysaccharide degradation
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
Molecular function	glucan 1,4-alpha-glucosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

22

Potential

Chain

936

Glucoamylase 1

PRO_0000018586

Regions

Compositional bias

16

Ser-rich

Compositional bias

13

Ser/Thr-rich

Sites

Active site

1

By similarity

Active site

1

By similarity

Active site

1

Proton donor By similarity

Amino acid modifications

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

P22861-1 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 47938DB9BC308260
Show »

958

106,508

        10         20         30         40         50         60 
MIFLKLIKSI VIGLGLVSAI QAAPASSIGS SASASSSSES SQATIPNDVT LGVKQIPNIF 

        70         80         90        100        110        120 
NDSAVDANAA AKGYDLVNVT NTPRGLTGIL KLKEATNIYG YDFDYLNLTV EYQADTRLNV 

       130        140        150        160        170        180 
HIEPTDLSDV FVLPEHLVVK PLVEGDAQSY NFDNSDLVFE YSNTDFSFEV IRSSTKEVLF 

       190        200        210        220        230        240 
STKGNPLVFS NQFIQFNSSL PKNHVITGLG ESIHGLVNEP GSVKTLFAND VGDPIDGNIY 

       250        260        270        280        290        300 
GVHPVYLDQR YDTETTHAVY WRTSAIQEVL IGEESITWRA LSGVIDLYFF SGPTPKDAIQ 

       310        320        330        340        350        360 
QYVKEIGLPA FQPYWSLGYH QCRWGYDTIE KLSEVVENFK KFNIPLETIW SDIDYMDSYK 

       370        380        390        400        410        420 
DFTYDPHRFP LDEYRKFLDE LHKNNQHYVP ILDAAIYVPN PNNATDNEYQ PFHYGNETDV 

       430        440        450        460        470        480 
FLKNPDGSLY IGAVWQVTLF SRFLSRKHSD MDKVIKDWYE LTPFDGIWAD MNEVSSFCVG 

       490        500        510        520        530        540 
SCGTGKYFEN PAYPPFTVGS KATSYPVGFD VSNASEWKSI QSSISATAKT SSTSSVSSSS 

       550        560        570        580        590        600 
STIDYMNTLA PGKGNINYPP YAIYNMQGDS DLATHAVSPN ATHADGTVEY DIHNLYGYLQ 

       610        620        630        640        650        660 
ENATYHALLE VFPNKRPFMI SRSTFPRAGK WTGHWGGDNT ADWAYAYFSI PQAFSMGIAG 

       670        680        690        700        710        720 
LPFFGADVCG FNGNSDSELC SRWMQLGSFF PFYRNHNYLG AIDQEPYVWE SVAEATRTSM 

       730        740        750        760        770        780 
AIRYLLLPYY YTLLHESHTT GLPILRAFSW QFPNDRSLSG VDNQFFVGDG LVVTPVLEPG 

       790        800        810        820        830        840 
VDKVKGVFPG AGKEEVYYDW YTQREVHFKD GKNETLDAPL GHIPLHIRGG NVLPTQEPGY 

       850        860        870        880        890        900 
TVAESRQNPF GLIVALDNDG KAQGSLYLDD GESLVVDSSL LVSFSVSDNT LSASPSGDYK 

       910        920        930        940        950 
ADQPLANVTI LGVGHKPKSV KFENANVDFT YKKSTVFVTG LDKYTKDGAF SKDFTITW

References

[1]	"Cloning of the Schwanniomyces occidentalis glucoamylase gene (GAM1) and its expression in Saccharomyces cerevisiae." Dohmen R.J., Strasser A.W.M., Dahlems U.M., Hollenberg C.P. Gene 95:111-121(1990) [PubMed: 1979298] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: ATCC 26076 / CBS 2864 / CCRC 22059 / NRRL Y-2470.
[2]	"Striking structural and functional similarities suggest that intestinal sucrase-isomaltase, human lysosomal alpha-glucosidase and Schwanniomyces occidentalis glucoamylase are derived from a common ancestral gene." Naim H.Y., Niermann T., Kleinhans U., Hollenberg C.P., Strasser A.W.M. FEBS Lett. 294:109-112(1991) [PubMed: 1743281] [Abstract] Cited for: SIMILARITY TO OTHER FAMILY 31 MEMBERS.

Cross-references

Sequence databases
	M60207 Genomic DNA. Translation: AAA33923.1.
PIR	JN0102.
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GH31. Glycoside Hydrolase Family 31.
Enzyme and pathway databases
BRENDA	3.2.1.3. 290444.
Family and domain databases
InterPro	IPR000322. Glyco_hydro_31. [Graphical view]
PANTHER	PTHR22762. Glyco_hydro_31. 1 hit.
Pfam	PF01055. Glyco_hydro_31. 1 hit. [Graphical view]
PROSITE	PS00129. GLYCOSYL_HYDROL_F31_1. 1 hit. PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMYG_DEBOC

Accession

Primary (citable) accession number: P22861
Secondary accession number(s): Q92336

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	April 14, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents