Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glucoamylase

Gene

gla

Organism
Aspergillus awamori (Black koji mold)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

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.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei143 – 1431SubstrateUniRule annotation
Active sitei199 – 1991Proton acceptorUniRule annotation
Active sitei202 – 2021Proton donorUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotationImported, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradationUniRule annotation

Enzyme and pathway databases

BRENDAi3.2.1.3. 494.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
GlucoamylaseUniRule annotation (EC:3.2.1.3UniRule annotation)
Alternative name(s):
1,4-alpha-D-glucan glucohydrolaseUniRule annotation
Glucan 1,4-alpha-glucosidaseUniRule annotation
Gene namesi
Name:glaImported
OrganismiAspergillus awamori (Black koji mold)Imported
Taxonomic identifieri105351 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Chaini19 – 639621GlucoamylaseSequence analysisPRO_5004181055Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ12537.
SMRiQ12537. Positions 25-639.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini532 – 639108CBM20 (carbohydrate binding type-20)InterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 15 family.UniRule annotation

Keywords - Domaini

SignalSequence analysis

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/PHK.
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.

Q12537-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFRSLLALS GLVCSGLASV 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 FGQWLLDNGY TSAATEIVWP LVRNDLSYVA QYWNQTGYDL
210 220 230 240 250
WEEVNGSSFF TIAVQHRALV EGSAFATAVG SSCSWCDSQA PQILCYLQSF
260 270 280 290 300
SSRSGWTGSY ILANFDKDTN TLLGSIHTFD PEAGCDDSTF QPCSPRALAN
310 320 330 340 350
HKEVVDSFRS IYTLNDGLSD SEAVAVGRYP EDSYYNGNPW FLCTLAAAEQ
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 SIVATGATTT
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):68,278
Last modified:November 1, 1996 - v1
Checksum:i6F93D0637D174ACB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59303 Genomic DNA. Translation: AAB02927.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59303 Genomic DNA. Translation: AAB02927.1.

3D structure databases

ProteinModelPortaliQ12537.
SMRiQ12537. Positions 25-639.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.3. 494.

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/PHK.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiQ12537_ASPAW
AccessioniPrimary (citable) accession number: Q12537
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: December 9, 2015
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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.