MALT_AEDAE
ID MALT_AEDAE Reviewed; 579 AA.
AC P13080; Q0IGE8; Q0IGE9;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 153.
DE RecName: Full=Probable maltase;
DE EC=3.2.1.20;
DE Flags: Precursor;
GN Name=MAL1; Synonyms=MAL I; ORFNames=AAEL000392;
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 / MRNA] (ISOFORM B).
RC STRAIN=Bahama, and Rockefeller; TISSUE=Salivary gland;
RX PubMed=2470653; DOI=10.1016/0378-1119(89)90384-3;
RA James A.A., Blackmer K., Racioppi J.V.;
RT "A salivary gland-specific, maltase-like gene of the vector mosquito, Aedes
RT aegypti.";
RL Gene 75:73-83(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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).
CC -!- FUNCTION: Assists the mosquito in its sugar-feeding capabilities
CC (Potential). Glucosidase (By similarity). {ECO:0000250, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-
CC glucose residues with release of alpha-D-glucose.; EC=3.2.1.20;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B;
CC IsoId=P13080-1; Sequence=Displayed;
CC Name=A;
CC IsoId=P13080-2; Sequence=VSP_027479;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; M30442; AAA29352.1; -; mRNA.
DR EMBL; M30443; AAA29351.1; -; Genomic_DNA.
DR EMBL; CH477192; EAT48589.1; -; Genomic_DNA.
DR EMBL; CH477192; EAT48590.1; -; Genomic_DNA.
DR PIR; JT0494; JT0494.
DR RefSeq; XP_001656069.1; XM_001656019.1.
DR RefSeq; XP_001656070.1; XM_001656020.1.
DR RefSeq; XP_001660189.1; XM_001660139.1. [P13080-1]
DR AlphaFoldDB; P13080; -.
DR SMR; P13080; -.
DR STRING; 7159.AAEL000392-PB; -.
DR Allergome; 11944; Aed a 4.0101.
DR Allergome; 1293; Aed a 4.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR GeneID; 5572111; -.
DR KEGG; aag:5572111; -.
DR VEuPathDB; VectorBase:AAEL009524; -.
DR eggNOG; KOG0471; Eukaryota.
DR HOGENOM; CLU_006462_2_3_1; -.
DR InParanoid; P13080; -.
DR OMA; FYQIHPE; -.
DR PhylomeDB; P13080; -.
DR Proteomes; UP000008820; Chromosome 3.
DR GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.90.400.10; -; 1.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR045857; O16G_dom_2.
DR Pfam; PF00128; Alpha-amylase; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..579
FT /note="Probable maltase"
FT /id="PRO_0000001451"
FT ACT_SITE 219
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 290
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT SITE 356
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..60
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000305"
FT /id="VSP_027479"
SQ SEQUENCE 579 AA; 66683 MW; 53760143F978672A CRC64;
MKIFVPLLSF LLAGLTTGLD WWEHGNFYQV YPRSFKDSDG DGIGDLDGVT EKLKYLKDIG
MDGVWLSPIF SSPMADFGYD ISNFREIQTE YGDLDAFQRL SDKCKQLGLH LILDFVPNHT
SDQHEYFKKS VQKDETYKDF YVWHPGVHGP NNTKVPPSNW ISVFRGSSWE WNEERQEFYL
HQFLKEQPDL NYRNPAVVEE MKNVLRYWLD RGVSGFRIDA VPYLFESDII DGRYRNEPES
RTTDDPENPA YLVHTQTMDQ PETYDMIYQW RAVLDEYSKT DNRTRIMMTE GYTSLPKIIE
FFGNATANGA QIPFNFEVIS NVKKNSTGAD FATYVKRWLD AKPANRRSNW VLGNHDNNRL
GSRLGENKID LYNIALQTLP DIAVTYYGEE IGMLDQWIPW NETVDPAACR SDEASYSAYS
RDPARTPMQW DSGKNAGFSK AAKTWLPVAD NYKTLNVKIQ DRARKSHLKI FKKLTKYRKR
QILTEGDIDI KVSGENLLVY KRKVDKVGYV VVALNFGTEP VALGLSSLFD RADQRMQVVV
SSNRVSTPDN VWVDVDNYVL IGESGIVLQY LWGKNPIVS
