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Protein

Alpha-amylase 1

Gene

LKA1

Organism
Lipomyces kononenkoae (Yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalytic activityi

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.2 Publications

Cofactori

Ca2+By similarityNote: Binds 2 calcium ions per subunit. Calcium is inhibitory at high concentrations.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei230SubstrateBy similarity1
Metal bindingi268Calcium 1By similarity1
Binding sitei269SubstrateBy similarity1
Metal bindingi309Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi322Calcium 1By similarity1
Binding sitei351SubstrateBy similarity1
Active sitei353NucleophileBy similarity1
Metal bindingi353Calcium 2By similarity1
Metal bindingi357Calcium 1; via carbonyl oxygenBy similarity1
Active sitei377Proton donorBy similarity1
Metal bindingi377Calcium 2By similarity1
Binding sitei381Substrate; via amide nitrogenBy similarity1
Binding sitei444SubstrateBy similarity1
Sitei444Transition state stabilizerBy similarity1
Binding sitei491SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism
LigandCalcium, Metal-binding

Protein family/group databases

CAZyiCBM21 Carbohydrate-Binding Module Family 21
GH13 Glycoside Hydrolase Family 13
mycoCLAPiAMY13A_LIPKO

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylase 1 (EC:3.2.1.12 Publications)
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase 1
Gene namesi
Name:LKA1
OrganismiLipomyces kononenkoae (Yeast)
Taxonomic identifieri34357 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesLipomycetaceaeLipomyces

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

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 281 PublicationAdd BLAST28
ChainiPRO_000000135429 – 624Alpha-amylase 1Add BLAST596

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi177 ↔ 185By similarity
Disulfide bondi297 ↔ 311By similarity
Glycosylationi304N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi344N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi387 ↔ 430By similarity
Disulfide bondi587 ↔ 622By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ01117

Structurei

3D structure databases

ProteinModelPortaliQ01117
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini40 – 133CBM21PROSITE-ProRule annotationAdd BLAST94

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni356 – 357Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.1180, 1 hit
2.60.40.2440, 1 hit
InterProiView protein in InterPro
IPR013777 A-amylase-like
IPR015340 A_amylase_DUF1966_C
IPR005036 CBM21_dom
IPR038175 CBM21_dom_sf
IPR006047 Glyco_hydro_13_cat_dom
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF00128 Alpha-amylase, 1 hit
PF09260 DUF1966, 1 hit
PIRSFiPIRSF001024 Alph-amyl_fung, 1 hit
SMARTiView protein in SMART
SM00642 Aamy, 1 hit
SUPFAMiSSF51445 SSF51445, 1 hit
PROSITEiView protein in PROSITE
PS51159 CBM21, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q01117-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLLINFFIAV LGVISLSPIV VARYILRRDC TTVTVLSSPE SVTGSNHVQL
60 70 80 90 100
ASYEMCGSTL SASLYVYNDD YDKIVTLYYL TSSGTTGSTL ALILPVWSNN
110 120 130 140 150
WELWTLSAIA AGAVEITGAS YVDSDTSVTY TTSLDLPLTT TSASVPTGTA
160 170 180 190 200
ANWRGRSIYQ VVTDRFARTD GSITYSCDVT DRVYCGGSYR GIINMLDYIQ
210 220 230 240 250
GMGFTAIWIS PIVENIPDDT GYGYAYHGYW MKDIFALNTN FGGADDLIAL
260 270 280 290 300
ATELHNRGMY LMVDIVVNHF AFSGNHADVD YSEYFPYSSQ DYFHSFCWIT
310 320 330 340 350
DYSNQTNVEE CWLGDDSVPL VDVNTQLDTV KSEYQSWVKQ LIANYSIDGL
360 370 380 390 400
RIDTVKHVQM DFWAPFQEAA GIYTVGEVFD GDPSYTCPYQ ENLDGVLNYP
410 420 430 440 450
VYYPVVSAFQ RVGGSISSLV DMIDTLKSEC IDTTLLGSFL ENQDNPRFPS
460 470 480 490 500
YTSDESLIKN AIAFTILSDG IPIIYYGQEQ GLNGGNDPYN REALWPTGYS
510 520 530 540 550
TTSTFYEYIA SLNQIRNHAI YIDDTYLTYQ NWVIYSDSTT IAMRKGFTGN
560 570 580 590 600
QIITVLSNLG SSGSSYTLTL SNTGYTASSV VYEILTCTAV TVDLSGNLAV
610 620
PMSGGLPRVF YPESQLVGSG ICSM
Length:624
Mass (Da):68,877
Last modified:November 1, 1998 - v2
Checksum:i87EB16534F5A9A9F
GO

Sequence cautioni

The sequence AAC49622 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30376 mRNA Translation: AAC49622.1 Different initiation.
PIRiJC4510

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30376 mRNA Translation: AAC49622.1 Different initiation.
PIRiJC4510

3D structure databases

ProteinModelPortaliQ01117
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM21 Carbohydrate-Binding Module Family 21
GH13 Glycoside Hydrolase Family 13
mycoCLAPiAMY13A_LIPKO

Proteomic databases

PRIDEiQ01117

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.60.40.1180, 1 hit
2.60.40.2440, 1 hit
InterProiView protein in InterPro
IPR013777 A-amylase-like
IPR015340 A_amylase_DUF1966_C
IPR005036 CBM21_dom
IPR038175 CBM21_dom_sf
IPR006047 Glyco_hydro_13_cat_dom
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF00128 Alpha-amylase, 1 hit
PF09260 DUF1966, 1 hit
PIRSFiPIRSF001024 Alph-amyl_fung, 1 hit
SMARTiView protein in SMART
SM00642 Aamy, 1 hit
SUPFAMiSSF51445 SSF51445, 1 hit
PROSITEiView protein in PROSITE
PS51159 CBM21, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiAMY1_LIPKO
AccessioniPrimary (citable) accession number: Q01117
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: November 1, 1998
Last modified: May 23, 2018
This is version 98 of the entry and version 2 of the sequence. See 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
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Main funding by: National Institutes of Health

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