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P23176

- AMYG_ASPKA

UniProt

P23176 - AMYG_ASPKA

Protein

Glucoamylase I

Gene

gaI

Organism
Aspergillus kawachii (White koji mold) (Aspergillus awamori var. kawachi)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Nov 1991)
      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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei143 – 1431SubstrateBy similarity
    Active sitei199 – 1991Proton acceptorPROSITE-ProRule annotation
    Active sitei202 – 2021Proton donorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. glucan 1,4-alpha-glucosidase activity Source: UniProtKB-EC
    2. starch binding Source: InterPro

    GO - Biological processi

    1. polysaccharide catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation

    Protein family/group databases

    CAZyiCBM20. Carbohydrate-Binding Module Family 20.
    GH15. Glycoside Hydrolase Family 15.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucoamylase I (EC:3.2.1.3)
    Alternative name(s):
    1,4-alpha-D-glucan glucohydrolase
    Glucan 1,4-alpha-glucosidase
    Gene namesi
    Name:gaI
    OrganismiAspergillus kawachii (White koji mold) (Aspergillus awamori var. kawachi)
    Taxonomic identifieri40384 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Add
    BLAST
    Propeptidei19 – 246PRO_0000001463
    Chaini25 – 639615Glucoamylase IPRO_0000001464Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi194 – 1941N-linked (GlcNAc...)By similarity
    Disulfide bondi233 ↔ 236By similarity
    Disulfide bondi245 ↔ 472By similarity
    Disulfide bondi285 ↔ 293By similarity
    Glycosylationi418 – 4181N-linked (GlcNAc...)By similarity
    Glycosylationi464 – 4641O-linked (Man)By similarity
    Glycosylationi466 – 4661O-linked (Man)By similarity
    Glycosylationi467 – 4671O-linked (Man)By similarity
    Glycosylationi475 – 4751O-linked (Man)By similarity
    Glycosylationi476 – 4761O-linked (Man)By similarity
    Glycosylationi482 – 4821O-linked (Man)By similarity
    Glycosylationi483 – 4831O-linked (Man)By similarity
    Glycosylationi485 – 4851O-linked (Man)By similarity
    Glycosylationi487 – 4871O-linked (Man)By similarity
    Glycosylationi491 – 4911O-linked (Man)By similarity
    Glycosylationi495 – 4951O-linked (Man)By similarity
    Glycosylationi498 – 4981O-linked (Man)By similarity
    Glycosylationi499 – 4991O-linked (Man)By similarity
    Glycosylationi500 – 5001O-linked (Man)By similarity
    Glycosylationi501 – 5011O-linked (Man)By similarity
    Glycosylationi503 – 5031O-linked (Man)By similarity
    Glycosylationi505 – 5051O-linked (Man)By similarity
    Glycosylationi507 – 5071O-linked (Man)By similarity
    Glycosylationi511 – 5111O-linked (Man)By similarity
    Glycosylationi512 – 5121O-linked (Man)By similarity
    Glycosylationi513 – 5131O-linked (Man)By similarity
    Glycosylationi514 – 5141O-linked (Man)By similarity
    Glycosylationi516 – 5161O-linked (Man)By similarity
    Glycosylationi517 – 5171O-linked (Man)By similarity
    Glycosylationi519 – 5191O-linked (Man)By similarity
    Glycosylationi521 – 5211O-linked (Man)By similarity
    Glycosylationi523 – 5231O-linked (Man)By similarity
    Glycosylationi524 – 5241O-linked (Man)By similarity
    Glycosylationi525 – 5251O-linked (Man)By similarity
    Glycosylationi526 – 5261O-linked (Man)By similarity
    Glycosylationi527 – 5271O-linked (Man)By similarity
    Glycosylationi528 – 5281O-linked (Man)By similarity
    Glycosylationi529 – 5291O-linked (Man)By similarity
    Glycosylationi530 – 5301O-linked (Man)By similarity
    Glycosylationi531 – 5311O-linked (Man)By similarity
    Glycosylationi533 – 5331O-linked (Man)By similarity
    Glycosylationi534 – 5341O-linked (Man)By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

    PTM databases

    UniCarbKBiP23176.

    Structurei

    3D structure databases

    ProteinModelPortaliP23176.
    SMRiP23176. Positions 25-639.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini532 – 639108CBM20PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni494 – 53138Raw-starch-adsorbable GP-I sequenceAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 15 family.Curated
    Contains 1 CBM20 (carbohydrate binding type-20) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di1.50.10.10. 1 hit.
    2.60.40.10. 1 hit.
    InterProiIPR008928. 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]
    PfamiPF00686. CBM_20. 1 hit.
    PF00723. Glyco_hydro_15. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001031. Glu-a-glcsd_SBD. 1 hit.
    PRINTSiPR00736. GLHYDRLASE15.
    SMARTiSM01065. CBM_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF48208. SSF48208. 1 hit.
    SSF49452. SSF49452. 1 hit.
    PROSITEiPS51166. CBM20. 1 hit.
    PS00820. GLUCOAMYLASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P23176-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSFRSLLALS GLVCSGLANV ISKRATLDSW LSNEATVART AILNNIGADG    50
    AWVSGADSGI VVASPSTDNP DYFYTWTRDS GLVIKTLVDL FRNGDTDLLS 100
    TIEHYISSQA IIQGVSNPSG DLSSGGLGEP KFNVDETAYT GSWGRPQRDG 150
    PALRATAMIG FGQVLLDNGY TSAATEIVWP LVRNDLSYVA QYWNQTGYDL 200
    WEEVNGSSFF TIAVQHRALV EGSAFATAVG SSCSWCDSQA PQILCYLQSF 250
    WTGSYILANF DSRRSGKDTN TLLGSIHTFD PEAGCDDSTF QPCSPRALAN 300
    HKEVVDSFRS IYTLNDGLSD SEAVAVGRYP EDSYYNGNPW FQSTLAAAEQ 350
    LYDALYQWDK QGSLEITDVS LDFFKALYSG AATGTYSSSS STYSSIVSAV 400
    KTFADGFVSI VETHAASNGS LSEQFDKSDG DELSARDLTW SYAALLTANN 450
    RRNSVVPPSW GETSASSWPG TCAATSASGT YSSVTVTSWP SIVATGGTTT 500
    TATTTGSGGV TSTSKTTTTA SKTSTTTSST SCTTPTAVAV TFDLTATTTY 550
    GENIYLVGSI SQLGDWETSD GIALSADKYT SSNPLWYVTV TLPAGESFEY 600
    KFIRVESDDS VEWESDPNRE YTVPQACGES TATVTDTWR 639
    Length:639
    Mass (Da):68,272
    Last modified:November 1, 1991 - v1
    Checksum:iE112B31A4DD8DD6B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00427 Genomic DNA. Translation: BAA00331.1.
    PIRiJT0479.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00427 Genomic DNA. Translation: BAA00331.1 .
    PIRi JT0479.

    3D structure databases

    ProteinModelPortali P23176.
    SMRi P23176. Positions 25-639.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM20. Carbohydrate-Binding Module Family 20.
    GH15. Glycoside Hydrolase Family 15.

    PTM databases

    UniCarbKBi P23176.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 1.50.10.10. 1 hit.
    2.60.40.10. 1 hit.
    InterProi 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 ]
    Pfami PF00686. CBM_20. 1 hit.
    PF00723. Glyco_hydro_15. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001031. Glu-a-glcsd_SBD. 1 hit.
    PRINTSi PR00736. GLHYDRLASE15.
    SMARTi SM01065. CBM_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48208. SSF48208. 1 hit.
    SSF49452. SSF49452. 1 hit.
    PROSITEi PS51166. CBM20. 1 hit.
    PS00820. GLUCOAMYLASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of the glucoamylase I gene of Aspergillus awamori var. kawachi for localization of the raw-starch-affinity site."
      Hayashida S., Kuroda K., Ohta K., Kuhara S., Fukuda K., Sakaki Y.
      Agric. Biol. Chem. 53:923-929(1989)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Structure of the raw-starch-affinity site on the Aspergillus awamori var. kawachi glucoamylase I molecule."
      Hayashida S., Nakahara K., Kuroda K., Miyata T., Iwanaga S.
      Agric. Biol. Chem. 53:135-141(1989)
      Cited for: PROTEIN SEQUENCE OF 494-538.

    Entry informationi

    Entry nameiAMYG_ASPKA
    AccessioniPrimary (citable) accession number: P23176
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 95 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3