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Protein

Glucoamylase 1

Gene

GAM1

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei462By similarity1
Active sitei465By similarity1
Active sitei628Proton donorBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

Protein family/group databases

CAZyiGH31. Glycoside Hydrolase Family 31.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucoamylase 1 (EC:3.2.1.3)
Alternative name(s):
1,4-alpha-D-glucan glucohydrolase
Glucan 1,4-alpha-glucosidase
Gene namesi
Name:GAM1
Synonyms:GCA1
ORF Names:CaO19.12365, CaO19.4899
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
Proteomesi
  • UP000000559 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000001858521 – 946Glucoamylase 1Add BLAST926

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi51N-linked (GlcNAc...)Sequence analysis1
Glycosylationi68N-linked (GlcNAc...)Sequence analysis1
Glycosylationi97N-linked (GlcNAc...)Sequence analysis1
Glycosylationi187N-linked (GlcNAc...)Sequence analysis1
Glycosylationi244N-linked (GlcNAc...)Sequence analysis1
Glycosylationi373N-linked (GlcNAc...)Sequence analysis1
Glycosylationi393N-linked (GlcNAc...)Sequence analysis1
Glycosylationi406N-linked (GlcNAc...)Sequence analysis1
Glycosylationi437N-linked (GlcNAc...)Sequence analysis1
Glycosylationi505N-linked (GlcNAc...)Sequence analysis1
Glycosylationi570N-linked (GlcNAc...)Sequence analysis1
Glycosylationi772N-linked (GlcNAc...)Sequence analysis1
Glycosylationi801N-linked (GlcNAc...)Sequence analysis1
Glycosylationi895N-linked (GlcNAc...)Sequence analysis1
Glycosylationi912N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiO74254.

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi519 – 532Ser/Thr-richAdd BLAST14

Sequence similaritiesi

Belongs to the glycosyl hydrolase 31 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

InParanoidiO74254.
KOiK01187.
OrthoDBiEOG092C0F23.

Family and domain databases

InterProiIPR031727. Gal_mutarotase_N.
IPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR030458. Glyco_hydro_31_AS.
IPR030459. Glyco_hydro_31_CS.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF01055. Glyco_hydro_31. 1 hit.
PF16863. NtCtMGAM_N. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
SSF74650. SSF74650. 1 hit.
PROSITEiPS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O74254-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLLSKVFVT ALGLTSIVNA APTSSSSAEE AQKTVPVELS IGVKQLPNIH
60 70 80 90 100
NDSAVDANAV AKGYSLVNVS LTARGLTGIL KLKEATNIYG YDFEYLNLSV
110 120 130 140 150
EYQSDTRLNV HIEPTDLTDV FVLPEELVVK PKLEGDAKTF NFENSDLVFE
160 170 180 190 200
YDEEDFGFEV LRSSTREVLF STKGNPLVFS NQFIQFNTTL PKGHSITGLG
210 220 230 240 250
ESIHGSLNEP GVVKTLYAND IADPIDGNIY GVHPVYYDQR YDTNTTHGVY
260 270 280 290 300
WRTSAIQEVV VGETSLTWRA LSGVIDLYFF SGPDPKDVIQ QYVSEIGLPA
310 320 330 340 350
MQPYWALGYH QCRWGYDTVE SLETVVENFK KFDIPLETIW SDIDYMDGYK
360 370 380 390 400
DFTNDPYRFP TDKFRKFLDD LHNNSQHYVP IFDAAIYVPN PNNATDDDYE
410 420 430 440 450
PFHLGNESDV FLKNPDGSLY IGAVWPGYTV FPDFLANNTQ EYWNKMFKDW
460 470 480 490 500
YERIPFDGIW TDMNEVSSFC VGSCGTGRYF DNPVHPPFEV GYSGSDYPLG
510 520 530 540 550
FDKSNASEWK SISEAAAATK TTTTTSSSTS TSIDGKNTLA PGKANINYPP
560 570 580 590 600
YAINNNQGDH GLATHAISPN ATHADGTVEY DIHNIYGLIQ ERAIYEALLE
610 620 630 640 650
IHPNKRPFII GRSSFAGSGK YMGHWGGDNY ADYYMMYFSI PQALSMGLSG
660 670 680 690 700
IPFFGVDACG FNGNTDMELC SRWMQLASFF PFYRNHNVLG AIPQEPYVWE
710 720 730 740 750
GVMNATKTSI NVRYSLLPYY YTLLHESHVT GIPIMRAFNW QFPYSKELAG
760 770 780 790 800
VDTQFFVGDA LLVTPVLEPG VNHTKGIFPG ENAVYYDFYT HKKQKFTAGK
810 820 830 840 850
NETLAAPLGH IPLHIKGGNI IPTQEPGYTT TESRKNPFGL LVALDAEGTA
860 870 880 890 900
SGKLYLDDGE SVDVEEALYV DFVASKNKLV ASVFGEYEVR QPLANVTILG
910 920 930 940
VDSEPKKVLF NNETVSHNYE NGAVYLTDLE KFTKEGAFAE EFSIQW
Length:946
Mass (Da):105,675
Last modified:October 19, 2011 - v2
Checksum:iA347712E0F974452
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti529T → A in AAC31968 (PubMed:10520161).Curated1
Sequence conflicti556N → D in AAC31968 (PubMed:10520161).Curated1
Sequence conflicti701G → A in AAC31968 (PubMed:10520161).Curated1
Sequence conflicti704N → K in AAC31968 (PubMed:10520161).Curated1
Sequence conflicti918N → K in AAC31968 (PubMed:10520161).Curated1
Sequence conflicti943 – 944SI → TL in AAC31968 (PubMed:10520161).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti7 – 8VF → FI in allele CaO19.12365. 2
Natural varianti102Y → S in allele CaO19.12365. 1
Natural varianti113E → D in allele CaO19.12365. 1
Natural varianti144N → T in allele CaO19.12365. 1
Natural varianti242D → N in allele CaO19.12365. 1
Natural varianti248G → A in allele CaO19.12365. 1
Natural varianti397D → N in allele CaO19.12365. 1
Natural varianti477G → D in allele CaO19.12365. 1
Natural varianti544A → G in allele CaO19.12365. 1
Natural varianti561G → D in allele CaO19.12365. 1
Natural varianti745S → N in allele CaO19.12365. 1
Natural varianti752D → E in allele CaO19.12365. 1
Natural varianti777I → V in allele CaO19.12365. 1
Natural varianti783A → V in allele CaO19.12365. 1
Natural varianti826P → A in allele CaO19.12365. 1
Natural varianti832E → G in allele CaO19.12365. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF082188 Genomic DNA. Translation: AAC31968.1.
AACQ01000001 Genomic DNA. Translation: EAL04887.1.
AACQ01000002 Genomic DNA. Translation: EAL04694.1.
RefSeqiXP_723393.1. XM_718300.1.
XP_723581.1. XM_718488.1.

Genome annotation databases

EnsemblFungiiEAL04694; EAL04694; CaO19.12365.
EAL04887; EAL04887; CaO19.4899.
GeneIDi3634903.
3635124.
KEGGical:CaO19.12365.
cal:CaO19.4899.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF082188 Genomic DNA. Translation: AAC31968.1.
AACQ01000001 Genomic DNA. Translation: EAL04887.1.
AACQ01000002 Genomic DNA. Translation: EAL04694.1.
RefSeqiXP_723393.1. XM_718300.1.
XP_723581.1. XM_718488.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH31. Glycoside Hydrolase Family 31.

Proteomic databases

PRIDEiO74254.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEAL04694; EAL04694; CaO19.12365.
EAL04887; EAL04887; CaO19.4899.
GeneIDi3634903.
3635124.
KEGGical:CaO19.12365.
cal:CaO19.4899.

Phylogenomic databases

InParanoidiO74254.
KOiK01187.
OrthoDBiEOG092C0F23.

Family and domain databases

InterProiIPR031727. Gal_mutarotase_N.
IPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR030458. Glyco_hydro_31_AS.
IPR030459. Glyco_hydro_31_CS.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF01055. Glyco_hydro_31. 1 hit.
PF16863. NtCtMGAM_N. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
SSF74650. SSF74650. 1 hit.
PROSITEiPS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAMYG_CANAL
AccessioniPrimary (citable) accession number: O74254
Secondary accession number(s): Q5AP64, Q5APQ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: October 19, 2011
Last modified: October 5, 2016
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Candida albicans
    Candida albicans: entries and gene names
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.