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Protein

Glucoamylase 1

Gene

GAM1

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed-Annotation score: -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

Sites

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

GO - Molecular functioni

GO - Biological processi

  • cell wall organization Source: UniProtKB-KW
  • polysaccharide catabolic process Source: UniProtKB-KW
  • single-species biofilm formation on inanimate substrate Source: CGD

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate 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
Ordered Locus Names:CAALFM_C110290WA
ORF Names:CaO19.12365, CaO19.4899
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
Proteomesi
  • UP000000559 Componenti: Chromosome 1

Organism-specific databases

CGDiCAL0000192588 GCA1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell wall, 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...) asparaginePROSITE-ProRule annotation1
Glycosylationi68N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi97N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi187N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi244N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi373N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi393N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi406N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi437N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi505N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi570N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi704N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi772N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi801N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi895N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi912N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

SMRiO74254
ModBaseiSearch...
MobiDBiSearch...

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

Gene3Di2.60.40.1180, 2 hits
InterProiView protein in InterPro
IPR031727 Gal_mutarotase_N
IPR011013 Gal_mutarotase_sf_dom
IPR000322 Glyco_hydro_31
IPR030458 Glyco_hydro_31_AS
IPR030459 Glyco_hydro_31_CS
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF01055 Glyco_hydro_31, 1 hit
PF16863 NtCtMGAM_N, 1 hit
SUPFAMiSSF51445 SSF51445, 2 hits
SSF74650 SSF74650, 1 hit
PROSITEiView protein in PROSITE
PS00129 GLYCOSYL_HYDROL_F31_1, 1 hit
PS00707 GLYCOSYL_HYDROL_F31_2, 1 hit

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 YNTNTTHAVY
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 PNNATDNDYE
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 PGKGNINYPP
560 570 580 590 600
YAINNNQGDH DLATHAISPN 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 VNHTKGVFPG 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):105,717
Last modified:March 15, 2017 - v3
Checksum:iD8A3D1BB2B7DD2B4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti242N → D in AAC31968 (PubMed:10520161).Curated1
Sequence conflicti248A → G in AAC31968 (PubMed:10520161).Curated1
Sequence conflicti397N → D in AAC31968 (PubMed:10520161).Curated1
Sequence conflicti477G → D in AAC31968 (PubMed:10520161).Curated1
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 conflicti777V → I in AAC31968 (PubMed:10520161).Curated1
Sequence conflicti918N → K in AAC31968 (PubMed:10520161).Curated1
Sequence conflicti943 – 944SI → TL in AAC31968 (PubMed:10520161).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF082188 Genomic DNA Translation: AAC31968.1
CP017623 Genomic DNA Translation: AOW26659.1
RefSeqiXP_723581.2, XM_718488.2

Genome annotation databases

EnsemblFungiiAOW26659; AOW26659; CAALFM_C110290WA
GeneIDi3634903
KEGGical:CAALFM_C110290WA

Similar proteinsi

Entry informationi

Entry nameiAMYG_CANAL
AccessioniPrimary (citable) accession number: O74254
Secondary accession number(s): A0A1D8PEU6, Q5AP64, Q5APQ9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: March 15, 2017
Last modified: May 23, 2018
This is version 85 of the entry and version 3 of the sequence. See 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

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