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P23176

- AMYG_ASPKA

UniProt

P23176 - AMYG_ASPKA

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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

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
Complete GO annotation...

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

        10         20         30         40         50
MSFRSLLALS GLVCSGLANV ISKRATLDSW LSNEATVART AILNNIGADG
60 70 80 90 100
AWVSGADSGI VVASPSTDNP DYFYTWTRDS GLVIKTLVDL FRNGDTDLLS
110 120 130 140 150
TIEHYISSQA IIQGVSNPSG DLSSGGLGEP KFNVDETAYT GSWGRPQRDG
160 170 180 190 200
PALRATAMIG FGQVLLDNGY TSAATEIVWP LVRNDLSYVA QYWNQTGYDL
210 220 230 240 250
WEEVNGSSFF TIAVQHRALV EGSAFATAVG SSCSWCDSQA PQILCYLQSF
260 270 280 290 300
WTGSYILANF DSRRSGKDTN TLLGSIHTFD PEAGCDDSTF QPCSPRALAN
310 320 330 340 350
HKEVVDSFRS IYTLNDGLSD SEAVAVGRYP EDSYYNGNPW FQSTLAAAEQ
360 370 380 390 400
LYDALYQWDK QGSLEITDVS LDFFKALYSG AATGTYSSSS STYSSIVSAV
410 420 430 440 450
KTFADGFVSI VETHAASNGS LSEQFDKSDG DELSARDLTW SYAALLTANN
460 470 480 490 500
RRNSVVPPSW GETSASSWPG TCAATSASGT YSSVTVTSWP SIVATGGTTT
510 520 530 540 550
TATTTGSGGV TSTSKTTTTA SKTSTTTSST SCTTPTAVAV TFDLTATTTY
560 570 580 590 600
GENIYLVGSI SQLGDWETSD GIALSADKYT SSNPLWYVTV TLPAGESFEY
610 620 630
KFIRVESDDS VEWESDPNRE YTVPQACGES TATVTDTWR
Length:639
Mass (Da):68,272
Last modified:November 1, 1991 - v1
Checksum:iE112B31A4DD8DD6B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00427 Genomic DNA. Translation: BAA00331.1.
PIRiJT0479.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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