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O74254

- AMYG_CANAL

UniProt

O74254 - AMYG_CANAL

Protein

Glucoamylase 1

Gene

GAM1

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 2 (19 Oct 2011)
      Previous versions | rss
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    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)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei462 – 4621By similarity
    Active sitei465 – 4651By similarity
    Active sitei628 – 6281Proton donorBy similarity

    GO - Molecular functioni

    1. alpha-1,4-glucosidase activity Source: CGD
    2. amylase activity Source: CGD
    3. carbohydrate binding Source: InterPro
    4. glucan 1,4-alpha-glucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate catabolic process Source: CGD
    2. filamentous growth Source: CGD
    3. filamentous growth of a population of unicellular organisms Source: CGD
    4. fungal-type cell wall polysaccharide biosynthetic process Source: CGD
    5. induction by symbiont of host immune response Source: CGD
    6. polysaccharide catabolic process Source: UniProtKB-KW
    7. single-species biofilm formation on inanimate substrate Source: CGD

    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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida
    ProteomesiUP000000559: Unassembled WGS sequence

    Organism-specific databases

    CGDiCAL0066397. GCA1.

    Subcellular locationi

    GO - Cellular componenti

    1. cell wall Source: UniProtKB-SubCell
    2. endoplasmic reticulum lumen Source: CGD
    3. extracellular region Source: CGD
    4. plasma membrane Source: CGD

    Keywords - Cellular componenti

    Membrane, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 946926Glucoamylase 1PRO_0000018585Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi51 – 511N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi68 – 681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi97 – 971N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi187 – 1871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi244 – 2441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi373 – 3731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi393 – 3931N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi406 – 4061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi437 – 4371N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi505 – 5051N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi570 – 5701N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi772 – 7721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi801 – 8011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi895 – 8951N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi912 – 9121N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    The N-terminus is blocked.

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi5476.CAL0005531.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi519 – 53214Ser/Thr-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 31 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1501.
    KOiK01187.
    OrthoDBiEOG77T1CZ.

    Family and domain databases

    InterProiIPR011013. Gal_mutarotase_SF_dom.
    IPR000322. Glyco_hydro_31.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF01055. Glyco_hydro_31. 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

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    MKLLSKVFVT ALGLTSIVNA APTSSSSAEE AQKTVPVELS IGVKQLPNIH    50
    NDSAVDANAV AKGYSLVNVS LTARGLTGIL KLKEATNIYG YDFEYLNLSV 100
    EYQSDTRLNV HIEPTDLTDV FVLPEELVVK PKLEGDAKTF NFENSDLVFE 150
    YDEEDFGFEV LRSSTREVLF STKGNPLVFS NQFIQFNTTL PKGHSITGLG 200
    ESIHGSLNEP GVVKTLYAND IADPIDGNIY GVHPVYYDQR YDTNTTHGVY 250
    WRTSAIQEVV VGETSLTWRA LSGVIDLYFF SGPDPKDVIQ QYVSEIGLPA 300
    MQPYWALGYH QCRWGYDTVE SLETVVENFK KFDIPLETIW SDIDYMDGYK 350
    DFTNDPYRFP TDKFRKFLDD LHNNSQHYVP IFDAAIYVPN PNNATDDDYE 400
    PFHLGNESDV FLKNPDGSLY IGAVWPGYTV FPDFLANNTQ EYWNKMFKDW 450
    YERIPFDGIW TDMNEVSSFC VGSCGTGRYF DNPVHPPFEV GYSGSDYPLG 500
    FDKSNASEWK SISEAAAATK TTTTTSSSTS TSIDGKNTLA PGKANINYPP 550
    YAINNNQGDH GLATHAISPN ATHADGTVEY DIHNIYGLIQ ERAIYEALLE 600
    IHPNKRPFII GRSSFAGSGK YMGHWGGDNY ADYYMMYFSI PQALSMGLSG 650
    IPFFGVDACG FNGNTDMELC SRWMQLASFF PFYRNHNVLG AIPQEPYVWE 700
    GVMNATKTSI NVRYSLLPYY YTLLHESHVT GIPIMRAFNW QFPYSKELAG 750
    VDTQFFVGDA LLVTPVLEPG VNHTKGIFPG ENAVYYDFYT HKKQKFTAGK 800
    NETLAAPLGH IPLHIKGGNI IPTQEPGYTT TESRKNPFGL LVALDAEGTA 850
    SGKLYLDDGE SVDVEEALYV DFVASKNKLV ASVFGEYEVR QPLANVTILG 900
    VDSEPKKVLF NNETVSHNYE NGAVYLTDLE KFTKEGAFAE EFSIQW 946
    Length:946
    Mass (Da):105,675
    Last modified:October 19, 2011 - v2
    Checksum:iA347712E0F974452
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti529 – 5291T → A in AAC31968. (PubMed:10520161)Curated
    Sequence conflicti556 – 5561N → D in AAC31968. (PubMed:10520161)Curated
    Sequence conflicti701 – 7011G → A in AAC31968. (PubMed:10520161)Curated
    Sequence conflicti704 – 7041N → K in AAC31968. (PubMed:10520161)Curated
    Sequence conflicti918 – 9181N → K in AAC31968. (PubMed:10520161)Curated
    Sequence conflicti943 – 9442SI → TL in AAC31968. (PubMed:10520161)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti7 – 82VF → FI in allele CaO19.12365.
    Natural varianti102 – 1021Y → S in allele CaO19.12365.
    Natural varianti113 – 1131E → D in allele CaO19.12365.
    Natural varianti144 – 1441N → T in allele CaO19.12365.
    Natural varianti242 – 2421D → N in allele CaO19.12365.
    Natural varianti248 – 2481G → A in allele CaO19.12365.
    Natural varianti397 – 3971D → N in allele CaO19.12365.
    Natural varianti477 – 4771G → D in allele CaO19.12365.
    Natural varianti544 – 5441A → G in allele CaO19.12365.
    Natural varianti561 – 5611G → D in allele CaO19.12365.
    Natural varianti745 – 7451S → N in allele CaO19.12365.
    Natural varianti752 – 7521D → E in allele CaO19.12365.
    Natural varianti777 – 7771I → V in allele CaO19.12365.
    Natural varianti783 – 7831A → V in allele CaO19.12365.
    Natural varianti826 – 8261P → A in allele CaO19.12365.
    Natural varianti832 – 8321E → G in allele CaO19.12365.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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

    GeneIDi3634903.
    3635124.
    KEGGical:CaO19.12365.
    cal:CaO19.4899.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF082188 Genomic DNA. Translation: AAC31968.1 .
    AACQ01000001 Genomic DNA. Translation: EAL04887.1 .
    AACQ01000002 Genomic DNA. Translation: EAL04694.1 .
    RefSeqi XP_723393.1. XM_718300.1.
    XP_723581.1. XM_718488.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5476.CAL0005531.

    Protein family/group databases

    CAZyi GH31. Glycoside Hydrolase Family 31.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 3634903.
    3635124.
    KEGGi cal:CaO19.12365.
    cal:CaO19.4899.

    Organism-specific databases

    CGDi CAL0066397. GCA1.

    Phylogenomic databases

    eggNOGi COG1501.
    KOi K01187.
    OrthoDBi EOG77T1CZ.

    Family and domain databases

    InterProi IPR011013. Gal_mutarotase_SF_dom.
    IPR000322. Glyco_hydro_31.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF01055. Glyco_hydro_31. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 2 hits.
    SSF74650. SSF74650. 1 hit.
    PROSITEi PS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
    PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and cloning of GCA1, a gene that encodes a cell surface glucoamylase from Candida albicans."
      Sturtevant J., Dixon F., Wadsworth E., Latge J.-P., Zhao X.-J., Calderone R.
      Med. Mycol. 37:357-366(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 193-213; 776-792 AND 817-835.
      Strain: SC5314 / ATCC MYA-2876.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: SC5314 / ATCC MYA-2876.

    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 1, 2014
    This is version 66 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

    External Data

    Dasty 3