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Protein

Alpha-amylase 1

Gene

LKA1

Organism
Lipomyces kononenkoae (Yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei230 – 2301SubstrateBy similarity
Metal bindingi268 – 2681Calcium 1By similarity
Binding sitei269 – 2691SubstrateBy similarity
Metal bindingi309 – 3091Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi322 – 3221Calcium 1By similarity
Binding sitei351 – 3511SubstrateBy similarity
Active sitei353 – 3531NucleophileBy similarity
Metal bindingi353 – 3531Calcium 2By similarity
Metal bindingi357 – 3571Calcium 1; via carbonyl oxygenBy similarity
Active sitei377 – 3771Proton donorBy similarity
Metal bindingi377 – 3771Calcium 2By similarity
Binding sitei381 – 3811Substrate; via amide nitrogenBy similarity
Binding sitei444 – 4441SubstrateBy similarity
Sitei444 – 4441Transition state stabilizerBy similarity
Binding sitei491 – 4911SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, 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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 28281 PublicationAdd
BLAST
Chaini29 – 624596Alpha-amylase 1PRO_0000001354Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi177 ↔ 185By similarity
Disulfide bondi297 ↔ 311By similarity
Glycosylationi304 – 3041N-linked (GlcNAc...)Sequence analysis
Glycosylationi344 – 3441N-linked (GlcNAc...)Sequence analysis
Disulfide bondi387 ↔ 430By similarity
Disulfide bondi587 ↔ 622By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ01117.
SMRiQ01117. Positions 148-623.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 13394CBM21PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni356 – 3572Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated
Contains 1 CBM21 (carbohydrate binding type-21) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR015340. A_amylase_DUF1966_C.
IPR005036. CBM21_dom.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF09260. DUF1966. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS51159. CBM21. 1 hit.
[Graphical view]

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 AAC49622.1 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.

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.
SMRiQ01117. Positions 148-623.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR015340. A_amylase_DUF1966_C.
IPR005036. CBM21_dom.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF09260. DUF1966. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS51159. CBM21. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning, sequence analysis and expression in yeasts of a cDNA containing a Lipomyces kononenkoae alpha-amylase-encoding gene."
    Steyn A.J.C., Marmur J., Pretorius I.S.
    Gene 166:65-71(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
    Strain: IGC4052B.
  2. "Characterization of a novel alpha-amylase from Lipomyces kononenkoae and expression of its gene (LKA1) in Saccharomyces cerevisiae."
    Steyn A.J.C., Pretorius I.S.
    Curr. Genet. 28:526-533(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 29-44, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
    Strain: IGC4052B.

Entry informationi

Entry nameiAMY1_LIPKO
AccessioniPrimary (citable) accession number: Q01117
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: November 1, 1998
Last modified: May 11, 2016
This is version 91 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

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

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.