AMY_HYPHA
ID AMY_HYPHA Reviewed; 485 AA.
AC A0A096XJN4;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 07-JAN-2015, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Alpha-amylase {ECO:0000255, ECO:0000255|RuleBase:RU361134, ECO:0000303|PubMed:25264343};
DE EC=3.2.1.1 {ECO:0000255, ECO:0000255|RuleBase:RU361134};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase {ECO:0000303|PubMed:25264343};
DE AltName: Full=AmyHha {ECO:0000303|PubMed:25264343};
DE Flags: Precursor;
GN Name=Amy {ECO:0000312|EMBL:AHY03307.1};
OS Hypothenemus hampei (Coffee berry borer).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Hypothenemus.
OX NCBI_TaxID=57062 {ECO:0000312|EMBL:AHY03307.1};
RN [1] {ECO:0000312|EMBL:AHY03307.1}
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, BIOTECHNOLOGY, AND
RP 3D-STRUCTURE MODELING.
RX PubMed=25264343; DOI=10.1016/j.gene.2014.09.050;
RA Bezerra C.A., Macedo L.L., Amorim T.M., Santos V.O., Fragoso R.R.,
RA Lucena W.A., Meneguim A.M., Valencia-Jimenez A., Engler G., Silva M.C.,
RA Albuquerque E.V., Grossi-de-Sa M.F.;
RT "Molecular cloning and characterization of an alpha-amylase cDNA highly
RT expressed in major feeding stages of the coffee berry borer, Hypothenemus
RT hampei.";
RL Gene 553:7-16(2014).
CC -!- FUNCTION: Involved in the digestion of starch (Probable).
CC {ECO:0000305|PubMed:25264343}.
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:0000255|RuleBase:RU361134};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P56634};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P56634};
CC -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996;
CC Evidence={ECO:0000250|UniProtKB:P56634};
CC Note=Binds 1 Cl(-) ion per subunit. {ECO:0000250|UniProtKB:P56634};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P56634}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in L2 larvae and adult insect
CC stages, which are the main feeding phases. Low levels are detected in
CC eggs and first instar (L1) stage, whereas a 200-fold increase is
CC observed at the second instar (L2) stage. Expression is significantly
CC reduced during the pupal stage, a period in which the insects do not
CC feed. After ecdysis, the expression increases again 200-fold during the
CC adult stage along with the resumed feeding.
CC {ECO:0000269|PubMed:25264343}.
CC -!- BIOTECHNOLOGY: A possible target of coffee bean insect pest control.
CC This important digestive enzyme could be for example knocked down using
CC the RNAi method. {ECO:0000303|PubMed:25264343}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000255|RuleBase:RU003615}.
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; KF963103; AHY03307.1; -; mRNA.
DR AlphaFoldDB; A0A096XJN4; -.
DR SMR; A0A096XJN4; -.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0031404; F:chloride ion binding; ISS:UniProtKB.
DR GO; GO:0005983; P:starch catabolic process; IEP:UniProtKB.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR006046; Alpha_amylase.
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; PF02806; Alpha-amylase_C; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 2: Evidence at transcript level;
KW Calcium; Carbohydrate metabolism; Chloride; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Metal-binding; Pyrrolidone carboxylic acid; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..485
FT /note="Alpha-amylase"
FT /evidence="ECO:0000255"
FT /id="PRO_5001926807"
FT ACT_SITE 202
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT ACT_SITE 238
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 200
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 301
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT SITE 303
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT MOD_RES 19
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 46..102
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 152..165
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 369..375
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 440..452
FT /evidence="ECO:0000250|UniProtKB:P56634"
SQ SEQUENCE 485 AA; 53124 MW; C55F9352DED81487 CRC64;
MQHLSILLVV LGSSIAFAQH DPHFADGRNT IVHLFGWKWG DIASECENWL RKKGFAGVQI
SPPSENPIVS GRPWWENYQP VSYDLKNRNG DEDSLSDMIK RCNNVGVRIY ADLVVNHMAT
SIGQGTADHS YDPGSKSYPA VPYSNENFHA SCDIDYNDAA SIRNCELSGL KDLDQSQDYV
RGKIVDYMNH LVSLGVAGFR VDAAKHMWPA DLAAIFGSVN DLNTDFFPSG SRAYIYQEVI
DTGSDPIDNK DYTGFGSVCE FKYGIQLATC FRGSNPLKYL ENWGTGWGLL DGGNTLVFID
NHDTERSSGS YLNYKESRAY KAANAFMLAH PYDGITKIMS SYDFSDNDQS PPSDGDNILS
PGFKEDGTCT NGWICQHRWS PIFNMVEFRS VVSGIELTNW WSGGDYQIAF SRGTKGTIAI
SINDSLDSDV PTGLPDGTYC DVISGSLSNG SCTGKSITVS GGKAHISIAS DDREAAVAIH
ANAKL
