AMY1_LIPKO
ID AMY1_LIPKO Reviewed; 624 AA.
AC Q01117;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Alpha-amylase 1;
DE EC=3.2.1.1 {ECO:0000269|PubMed:8529895, ECO:0000269|PubMed:8593683};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase 1;
DE Flags: Precursor;
GN Name=LKA1;
OS Lipomyces kononenkoae (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Lipomycetaceae; Lipomyces.
OX NCBI_TaxID=34357;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC STRAIN=IGC4052B;
RX PubMed=8529895; DOI=10.1016/0378-1119(95)00633-0;
RA Steyn A.J.C., Marmur J., Pretorius I.S.;
RT "Cloning, sequence analysis and expression in yeasts of a cDNA containing a
RT Lipomyces kononenkoae alpha-amylase-encoding gene.";
RL Gene 166:65-71(1995).
RN [2]
RP PROTEIN SEQUENCE OF 29-44, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC STRAIN=IGC4052B;
RX PubMed=8593683; DOI=10.1007/bf00518165;
RA Steyn A.J.C., Pretorius I.S.;
RT "Characterization of a novel alpha-amylase from Lipomyces kononenkoae and
RT expression of its gene (LKA1) in Saccharomyces cerevisiae.";
RL Curr. Genet. 28:526-533(1995).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000269|PubMed:8529895,
CC ECO:0000269|PubMed:8593683};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P0C1B3};
CC Note=Binds 2 calcium ions per subunit. Calcium is inhibitory at high
CC concentrations. {ECO:0000250|UniProtKB:P0C1B3};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8529895,
CC ECO:0000269|PubMed:8593683}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC49622.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U30376; AAC49622.1; ALT_INIT; mRNA.
DR PIR; JC4510; JC4510.
DR AlphaFoldDB; Q01117; -.
DR SMR; Q01117; -.
DR CAZy; CBM21; Carbohydrate-Binding Module Family 21.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR CLAE; AMY13A_LIPKO; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR013777; A-amylase-like.
DR InterPro; IPR015340; A_amylase_C_dom.
DR InterPro; IPR005036; CBM21_dom.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF09260; DUF1966; 1.
DR PIRSF; PIRSF001024; Alph-amyl_fung; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS51159; CBM21; 1.
PE 1: Evidence at protein level;
KW Calcium; Carbohydrate metabolism; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Metal-binding;
KW Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:8593683"
FT CHAIN 29..624
FT /note="Alpha-amylase 1"
FT /id="PRO_0000001354"
FT DOMAIN 40..133
FT /note="CBM21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00491"
FT ACT_SITE 353
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT ACT_SITE 377
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 268
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT BINDING 322
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 353
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 356..357
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 357
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 377
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 381
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 444
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 491
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT SITE 444
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 177..185
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT DISULFID 297..311
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT DISULFID 387..430
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT DISULFID 587..622
FT /evidence="ECO:0000250|UniProtKB:P56271"
SQ SEQUENCE 624 AA; 68877 MW; 87EB16534F5A9A9F CRC64;
MLLINFFIAV LGVISLSPIV VARYILRRDC TTVTVLSSPE SVTGSNHVQL ASYEMCGSTL
SASLYVYNDD YDKIVTLYYL TSSGTTGSTL ALILPVWSNN WELWTLSAIA AGAVEITGAS
YVDSDTSVTY TTSLDLPLTT TSASVPTGTA ANWRGRSIYQ VVTDRFARTD GSITYSCDVT
DRVYCGGSYR GIINMLDYIQ GMGFTAIWIS PIVENIPDDT GYGYAYHGYW MKDIFALNTN
FGGADDLIAL ATELHNRGMY LMVDIVVNHF AFSGNHADVD YSEYFPYSSQ DYFHSFCWIT
DYSNQTNVEE CWLGDDSVPL VDVNTQLDTV KSEYQSWVKQ LIANYSIDGL RIDTVKHVQM
DFWAPFQEAA GIYTVGEVFD GDPSYTCPYQ ENLDGVLNYP VYYPVVSAFQ RVGGSISSLV
DMIDTLKSEC IDTTLLGSFL ENQDNPRFPS YTSDESLIKN AIAFTILSDG IPIIYYGQEQ
GLNGGNDPYN REALWPTGYS TTSTFYEYIA SLNQIRNHAI YIDDTYLTYQ NWVIYSDSTT
IAMRKGFTGN QIITVLSNLG SSGSSYTLTL SNTGYTASSV VYEILTCTAV TVDLSGNLAV
PMSGGLPRVF YPESQLVGSG ICSM
