AMY1_AEDAE
ID AMY1_AEDAE Reviewed; 737 AA.
AC P53354; O02413; Q175A0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Alpha-amylase I;
DE EC=3.2.1.1 {ECO:0000250|UniProtKB:P56634};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE Flags: Precursor;
GN Name=AMY1; Synonyms=AMY I; ORFNames=AAEL006719;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Rockefeller;
RX PubMed=9443377; DOI=10.1016/s0965-1748(97)00063-5;
RA Grossman G.L., Campos Y., Severson D.W., James A.A.;
RT "Evidence for two distinct members of the amylase gene family in the yellow
RT fever mosquito, Aedes aegypti.";
RL Insect Biochem. Mol. Biol. 27:769-781(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-726, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF
RP 1-13 AND 722-737, AND TISSUE SPECIFICITY.
RC STRAIN=Rockefeller; TISSUE=Salivary gland;
RX PubMed=7505701; DOI=10.1111/j.1365-2583.1993.tb00095.x;
RA Grossman G.L., James A.A.;
RT "The salivary glands of the vector mosquito, Aedes aegypti, express a novel
RT member of the amylase gene family.";
RL Insect Mol. Biol. 1:223-232(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; Evidence={ECO:0000250|UniProtKB:P56634};
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}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed specifically in the proximal-lateral
CC lobes of the adult female salivary gland. {ECO:0000269|PubMed:7505701}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; AF000569; AAB60935.1; -; Genomic_DNA.
DR EMBL; CH477404; EAT41631.1; -; Genomic_DNA.
DR EMBL; L03637; AAA29343.1; -; mRNA.
DR EMBL; L03638; AAA29344.1; -; mRNA.
DR EMBL; L03639; AAA29345.1; -; Genomic_DNA.
DR EMBL; L03640; AAA29346.1; -; Genomic_DNA.
DR RefSeq; XP_001652172.1; XM_001652122.1.
DR AlphaFoldDB; P53354; -.
DR SMR; P53354; -.
DR STRING; 7159.AAEL006719-PA; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR GeneID; 5568295; -.
DR KEGG; aag:5568295; -.
DR VEuPathDB; VectorBase:AAEL006719; -.
DR eggNOG; KOG2212; Eukaryota.
DR HOGENOM; CLU_376535_0_0_1; -.
DR InParanoid; P53354; -.
DR OMA; VSPINEY; -.
DR OrthoDB; 665362at2759; -.
DR PhylomeDB; P53354; -.
DR Proteomes; UP000008820; Chromosome 2.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..737
FT /note="Alpha-amylase I"
FT /id="PRO_0000001359"
FT REGION 17..260
FT /note="Not found in other alpha-amylases"
FT REGION 87..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 447
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT ACT_SITE 484
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 356
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 408
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 417
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 445
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 451
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 550
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 589
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT SITE 552
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 595
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 619
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 673
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 286..342
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 396..410
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 622..628
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 693..705
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT CONFLICT 19
FT /note="L -> F (in Ref. 3; AAA29343)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="R -> H (in Ref. 3; AAA29343)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="G -> A (in Ref. 3; AAA29343)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="N -> K (in Ref. 1; AAB60935)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="M -> I (in Ref. 1; AAB60935 and 3; AAA29343)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="K -> T (in Ref. 1; AAB60935)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="A -> D (in Ref. 3; AAA29343)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="M -> I (in Ref. 1; AAB60935)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="L -> V (in Ref. 1; AAB60935)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="N -> K (in Ref. 1; AAB60935 and 3; AAA29343)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="Q -> L (in Ref. 1; AAB60935)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="R -> Q (in Ref. 3; AAA29343)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="V -> D (in Ref. 1; AAB60935 and 3; AAA29343)"
FT /evidence="ECO:0000305"
FT CONFLICT 512
FT /note="A -> V (in Ref. 1; AAB60935 and 3; AAA29343)"
FT /evidence="ECO:0000305"
FT CONFLICT 571
FT /note="R -> P (in Ref. 1; AAB60935 and 3; AAA29343)"
FT /evidence="ECO:0000305"
FT CONFLICT 612
FT /note="K -> R (in Ref. 1; AAB60935 and 3; AAA29343)"
FT /evidence="ECO:0000305"
FT CONFLICT 617
FT /note="A -> V (in Ref. 1; AAB60935 and 3; AAA29343)"
FT /evidence="ECO:0000305"
FT CONFLICT 618
FT /note="A -> V (in Ref. 1; AAB60935)"
FT /evidence="ECO:0000305"
FT CONFLICT 624
FT /note="N -> T (in Ref. 1; AAB60935 and 3; AAA29343)"
FT /evidence="ECO:0000305"
FT CONFLICT 727
FT /note="I -> V (in Ref. 1; AAB60935 and 3; AAA29345)"
FT /evidence="ECO:0000305"
FT CONFLICT 732
FT /note="V -> I (in Ref. 1; AAB60935 and 3; AAA29345)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 737 AA; 80891 MW; 682A1F42055AC753 CRC64;
MKQLLVILYS ALVVTNAQLP GFSFGPSGFG GFSLSNPLFN ASFAPANPVD RISDIASRFR
DVANNVQRNL PKIPQFTNPL SAFSRFARPT SSSGSTNANS NNNQNFNSNQ ANEGTSGARN
AINEVLNRIP GLSGVPRVPE IPKVPEIPSF GNPSDVFGPF VNSLRNMTNQ GINDPGQMFN
QVNKFLPDVS RIANSVANYA KSAANSGIWK NISNDIKHEM QNRIESMTQM LSNITSAMKN
IAQSLPNLMQ DQSLNTTLRN QPFFFPGHSG IVHLFEWKFS DIAEECENVL GPNGYGGVQV
SPINEYLVSP SRAWWERYQP ISFEIKSRSG NEKQFSDMVK RCMKAGVRIY VDVVVNHMAA
PGASAPLYGT AGSTCDPQAR DYPGVPFNRS HFHADCQIND YNNATNVRNC ELAALPDLDQ
SNRFVQNKII QYLNHLLDLG VAGFRMDACK HMRPEDLKSI YVRLKPVNAM FLFPPGARPF
IFQEVIDLGT EGVSAKEYTN LGVVTEFNWC IAVGGVFRGT TNADALELLT KNGSAGVLLP
SSQALVFVDN HDNQRGHGAG GDSILTYKTK RQYIQAVAFT LATDYGIARV MSSYNFSDPD
QGPPQDTVQV IKSPGFAANN SCSNGWVCEH RWPEIRKMIQ FKNFVAGSSL DHIQATQNTF
AFCRGEKGFI VFNNSENTIT QQYHTCLPQG QYCDIISGEV SQSTCTGTVV NVDANGDAEI
TLPKNSIVAI YVPSRLS
