Reviewed, UniProtKB/Swiss-Prot Q01117 (AMY1_LIPKO)

Names and origin

Protein names

Recommended name:
    Alpha-amylase 1
    EC=3.2.1.1
Alternative name(s):
    1,4-alpha-D-glucan glucanohydrolase 1

Gene names

Name:

LKA1

Organism

Lipomyces kononenkoae

Taxonomic identifier

34357 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Lipomycetaceae › Lipomyces

Protein attributes

Sequence length	624 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides.
Cofactor	Binds 2 calcium ions per subunit. Calcium is inhibitory at high concentrations By similarity.
Subcellular location	Secreted.
Sequence similarities	Belongs to the glycosyl hydrolase 13 family. Contains 1 CBM21 (carbohydrate binding type-21) domain.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	alpha-amylase activity Inferred from electronic annotation. Source: EC calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 28	28	Ref.2
	Chain	29 – 624	596	Alpha-amylase 1		PRO_0000001354
Regions
	Domain	40 – 133	94	CBM21
Sites
	Active site	353	1	Nucleophile By similarity
	Active site	377	1	Proton donor By similarity
	Active site	444	1	By similarity
	Metal binding	268	1	Calcium 1 By similarity
	Metal binding	309	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	322	1	Calcium 1 By similarity
	Metal binding	353	1	Calcium 2 By similarity
	Metal binding	357	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	377	1	Calcium 2 By similarity
Amino acid modifications
	Glycosylation	304	1	N-linked (GlcNAc...) Potential
	Glycosylation	344	1	N-linked (GlcNAc...) Potential
	Disulfide bond	177 ↔ 185		By similarity
	Disulfide bond	297 ↔ 311		By similarity
	Disulfide bond	387 ↔ 430		By similarity
	Disulfide bond	587 ↔ 622		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q01117-1 [UniParc]. Last modified November 1, 1998. Version 2. Checksum: 87EB16534F5A9A9F	FASTA	624	68,877
	10 20 30 40 50 60 MLLINFFIAV LGVISLSPIV VARYILRRDC TTVTVLSSPE SVTGSNHVQL ASYEMCGSTL 70 80 90 100 110 120 SASLYVYNDD YDKIVTLYYL TSSGTTGSTL ALILPVWSNN WELWTLSAIA AGAVEITGAS 130 140 150 160 170 180 YVDSDTSVTY TTSLDLPLTT TSASVPTGTA ANWRGRSIYQ VVTDRFARTD GSITYSCDVT 190 200 210 220 230 240 DRVYCGGSYR GIINMLDYIQ GMGFTAIWIS PIVENIPDDT GYGYAYHGYW MKDIFALNTN 250 260 270 280 290 300 FGGADDLIAL ATELHNRGMY LMVDIVVNHF AFSGNHADVD YSEYFPYSSQ DYFHSFCWIT 310 320 330 340 350 360 DYSNQTNVEE CWLGDDSVPL VDVNTQLDTV KSEYQSWVKQ LIANYSIDGL RIDTVKHVQM 370 380 390 400 410 420 DFWAPFQEAA GIYTVGEVFD GDPSYTCPYQ ENLDGVLNYP VYYPVVSAFQ RVGGSISSLV 430 440 450 460 470 480 DMIDTLKSEC IDTTLLGSFL ENQDNPRFPS YTSDESLIKN AIAFTILSDG IPIIYYGQEQ 490 500 510 520 530 540 GLNGGNDPYN REALWPTGYS TTSTFYEYIA SLNQIRNHAI YIDDTYLTYQ NWVIYSDSTT 550 560 570 580 590 600 IAMRKGFTGN QIITVLSNLG SSGSSYTLTL SNTGYTASSV VYEILTCTAV TVDLSGNLAV 610 620 PMSGGLPRVF YPESQLVGSG ICSM

References

[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: 8529895] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 8593683] [Abstract] Cited for: PROTEIN SEQUENCE OF 29-44. Strain: IGC4052B.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U30376 mRNA. Translation: AAC49622.1. Different initiation.
PIR	JC4510.
3D structure databases
SMR	Q01117. Positions 148-623.
ModBase	Search...
Protein family/group databases
CAZy	CBM21. Carbohydrate-Binding Module Family 21. GH13. Glycoside Hydrolase Family 13.
Enzyme and pathway databases
BRENDA	3.2.1.1. 97343.
Family and domain databases
InterPro	IPR013777. A-amylase_fun. IPR015340. A_amylase_DUF1966_C. IPR005036. CBM_21. IPR013780. Glyco_hydro_13_b. IPR006047. Glyco_hydro_13_cat_dom. IPR006589. Glyco_hydro_13_sub_cat_dom. IPR017853. Glyco_hydro_catalytic_core. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF00128. Alpha-amylase. 1 hit. PF09260. DUF1966. 1 hit. [Graphical view]
PIRSF	PIRSF001024. Alph-amyl_fung. 1 hit.
SMART	SM00642. Aamy. 1 hit. [Graphical view]
PROSITE	PS51159. CBM21. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMY1_LIPKO

Accession

Primary (citable) accession number: Q01117

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2003
Last sequence update:	November 1, 1998
Last modified:	January 19, 2010
This is version 62 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)