AMY2_SCHOC
ID AMY2_SCHOC Reviewed; 507 AA.
AC Q08806;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Alpha-amylase 2;
DE EC=3.2.1.1;
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase 2;
DE Flags: Precursor;
GN Name=SWA2;
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].
RC STRAIN=ATCC 26077 / CBS 2863 / JCM 8124 / BCRC 20332 / NBRC 1840 / NRRL
RC Y-2477;
RX PubMed=8358835; DOI=10.1007/bf00324668;
RA Claros M.G., Abarca D., Fernandez-Lobato M., Jimenez A.;
RT "Molecular structure of the SWA2 gene encoding an AMY1-related alpha-
RT amylase from Schwanniomyces occidentalis.";
RL Curr. Genet. 24:75-83(1993).
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;
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X73497; CAA51912.1; -; Genomic_DNA.
DR PIR; S33921; S33921.
DR AlphaFoldDB; Q08806; -.
DR SMR; Q08806; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR CLAE; AMY13B_DEBOC; -.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
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 3: Inferred from homology;
KW Calcium; Carbohydrate metabolism; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Metal-binding; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..507
FT /note="Alpha-amylase 2"
FT /id="PRO_0000001353"
FT ACT_SITE 238
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT ACT_SITE 262
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 238
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 241..242
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="1"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 329
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 376
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT SITE 329
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 62..70
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT DISULFID 182..196
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT DISULFID 272..315
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT DISULFID 470..505
FT /evidence="ECO:0000250|UniProtKB:P56271"
SQ SEQUENCE 507 AA; 55967 MW; 3A562E95BD8AAD63 CRC64;
MKFATILSTT ALALSSLVAS KPIFLSKRDA GSSAAAAWRS ESIYQLVTDR FARTDGSTSA
TCNTGDRVYC GGTFQGIIDK LDYIQGMGFT AIWISPVVEQ IPDDTGYGYA YHGYWMKDIY
AINSNFGTAD DLKNLSNELH KRNMKLMVDI VTNHYAWNGA GSSVAYSNYN PFNQQSYFHD
YCLITNYDDQ TNVEDCWEGD NTVSLPDLRT EDSDVSSIFN LWVAELVSNY SIDGLRIDSA
KHVDESFYPS FQSAAGVYLL GEVYDGDPAY TCPYQNYMSG VTNYPLYYPM LRFFQGTSNS
VDELNAMISS LESDCKDITL LGNFIENHDQ PRLPSYTSDS ALIKNAIAFN LMSDGIPIIY
YGQEQGYSGS SDPNNREALW LSGYSTSNGY YKLISSVNQI RNQAIYKDSK YTTYWSDVLY
ASGHVIALQR GADDQRIVSV FNNLGSSGSQ TVTFSTKYSG GEKVVDVLTC QTSYANSDST
LTVSISGGAP RIYAPASLIA NSGICNF
