AMY1_SCHOC
ID AMY1_SCHOC Reviewed; 512 AA.
AC P19269;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Alpha-amylase 1;
DE EC=3.2.1.1 {ECO:0000269|PubMed:2806251};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase 1;
DE Flags: Precursor;
GN Name=AMY1;
OS Schwanniomyces occidentalis (Yeast) (Debaryomyces occidentalis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Schwanniomyces.
OX NCBI_TaxID=27300;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 26076 / DSM 3794 / CBS 2864 / BCRC 22059 / NCYC 954 / NRRL
RC Y-2470;
RX PubMed=2806251; DOI=10.1111/j.1432-1033.1989.tb15069.x;
RA Strasser A.W.M., Selk R., Dohmen R.J., Niermann T., Bielefeld M.,
RA Seeboth P., Tu G., Hollenberg C.P.;
RT "Analysis of the alpha-amylase gene of Schwanniomyces occidentalis and the
RT secretion of its gene product in transformants of different yeast genera.";
RL Eur. J. Biochem. 184:699-706(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BCRC 21164;
RX PubMed=1769525; DOI=10.1016/0378-1097(91)90280-n;
RA Wu F.M., Wang T.T., Hsu W.H.;
RT "The nucleotide sequence of Schwanniomyces occidentalis alpha-amylase
RT gene.";
RL FEMS Microbiol. Lett. 66:313-318(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 26077 / CBS 2863 / JCM 8124 / BCRC 20332 / NBRC 1840 / NRRL
RC Y-2477;
RX PubMed=1612414; DOI=10.1016/0378-1097(92)90483-5;
RA Park J.C., Bai S., Tai C.Y., Chun S.B.;
RT "Nucleotide sequence of the extracellular alpha-amylase gene in the yeast
RT Schwanniomyces occidentalis ATCC 26077.";
RL FEMS Microbiol. Lett. 72:17-23(1992).
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:2806251};
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 -!- ACTIVITY REGULATION: Alpha-amylase expression underlies catabolite
CC repression by glucose.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2806251}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; S77586; AAB21151.2; -; Genomic_DNA.
DR EMBL; X16040; CAA34162.1; -; Genomic_DNA.
DR EMBL; X62079; CAA43995.1; -; Genomic_DNA.
DR EMBL; S38381; AAB22383.2; -; Genomic_DNA.
DR PIR; S06115; S06115.
DR PIR; S23355; S23355.
DR AlphaFoldDB; P19269; -.
DR SMR; P19269; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
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; 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.
PE 1: Evidence at protein level;
KW Calcium; Carbohydrate metabolism; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Metal-binding; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..512
FT /note="Alpha-amylase 1"
FT /id="PRO_0000001352"
FT ACT_SITE 242
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT ACT_SITE 266
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 245..246
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 266
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 333
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 380
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT SITE 333
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 66..74
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT DISULFID 186..200
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT DISULFID 276..319
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT DISULFID 475..510
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT VARIANT 32
FT /note="M -> K (in strain: CCRC 21164 and ATCC 26077 / CBS
FT 2863)"
FT VARIANT 36
FT /note="S -> G (in strain: CCRC 21164)"
FT VARIANT 73
FT /note="Y -> I (in strain: ATCC 26077 / CBS 2863)"
FT VARIANT 280
FT /note="N -> S (in strain: CCRC 21164)"
FT VARIANT 350
FT /note="D -> A (in strain: CCRC 21164 and ATCC 26077 / CBS
FT 2863)"
FT VARIANT 479
FT /note="L -> S (in strain: CCRC 21164 and ATCC 26077 / CBS
FT 2863)"
FT VARIANT 483
FT /note="S -> F (in strain: CCRC 21164)"
SQ SEQUENCE 512 AA; 56527 MW; 857552B2CF60F965 CRC64;
MRFSTEGFTS KVVAAILAFS RLVSAQPIIF DMRDVSSSAD KWKDQSIYQI VTDRFARSDG
STTADCLVSD RKYCGGSYKG IIDKLDYIQG MGFTAIWISP VVEQIPDNTA YGYAYHGYWM
KNIDELNTNF GTADELKQLA SELHSRSMLL MVDVVYNHYA WNGDGSSVDY SSFTPFNQQS
YFHDYCLITN YNDQTNVEDC WEGDTEVSLP DLSTEDNEVI GVFQTWVSDF VQNYSIDGLR
IDSAKHVDTA SLTKFEDASG VYNLGEVYQG DPTYTCPYQN YMKGVTNYPL YYPVYRFFSD
TSATSSELTS MISTLQSSCS DVSLLGNFIE NHDQVRFPSV TSDTSLIKND MAFIILGDGI
PIIYYGQEQG LNGGSDPANR EALWLSGYNT DSEYYELISK LNQIRNQAIK KDSAYSTYKS
SVVSSSDHYI ATRKGSDANQ LISIFNNLGS NGSQDITVSN TGYSSGDKVI DIISCNSVLA
GDSGSLSVSI SGGMPQVYAP SSVLSGSGIC NQ
