ID   MAL1_DROVI              Reviewed;         632 AA.
AC   O16098; B4LQJ1;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 125.
DE   RecName: Full=Maltase 1;
DE            EC=3.2.1.20;
DE   Flags: Precursor;
GN   Name=Mal-B1; Synonyms=Mav1; ORFNames=GJ22501;
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15010-1051.87;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 71-632.
RC   STRAIN=9;
RX   PubMed=9335139; DOI=10.1093/oxfordjournals.molbev.a025715;
RA   Vieira C.P., Vieira J., Hartl D.L.;
RT   "The evolution of small gene clusters: evidence for an independent origin
RT   of the maltase gene cluster in Drosophila virilis and Drosophila
RT   melanogaster.";
RL   Mol. Biol. Evol. 14:985-993(1997).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB82327.1; Type=Miscellaneous discrepancy; Note=Several sequencing errors.; Evidence={ECO:0000305};
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DR   EMBL; CH940649; EDW64448.1; -; Genomic_DNA.
DR   EMBL; AF006573; AAB82327.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_002052293.2; XM_002052257.2.
DR   AlphaFoldDB; O16098; -.
DR   SMR; O16098; -.
DR   STRING; 7244.O16098; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GlyCosmos; O16098; 6 sites, No reported glycans.
DR   EnsemblMetazoa; FBtr0439930; FBpp0396571; FBgn0022839.
DR   GeneID; 6627887; -.
DR   KEGG; dvi:6627887; -.
DR   eggNOG; KOG0471; Eukaryota.
DR   HOGENOM; CLU_006462_8_3_1; -.
DR   InParanoid; O16098; -.
DR   OMA; NWWRHEV; -.
DR   OrthoDB; 3680211at2759; -.
DR   PhylomeDB; O16098; -.
DR   Proteomes; UP000008792; Unassembled WGS sequence.
DR   GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
DR   CDD; cd11328; AmyAc_maltase; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR045857; O16G_dom_2.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF235; ALPHA-GLUCOSIDASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Signal.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..632
FT                   /note="Maltase 1"
FT                   /id="PRO_0000001449"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        280
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        348
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   SITE            415
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        179
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        212
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        333
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        461
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        575
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        578
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   632 AA;  72991 MW;  5182C968F730CE0E CRC64;
     MEEGERWREG HVYQRSSETR KPTNYDRPDS PVTHYVSDTH IVGTLMDELE VETGLITTIL
     IATFNEMRRS HKPNELDDNI NWWRHEVFYQ IYPRSFKDSD GDGIGDLKGI TSKLQYFVDT
     GITAIWLSPI YKSPMVDFGY DISDYRDIQP EYGTLEDFDA LIAKANQLGI KVILDFVPNH
     SSDEHEWFKK SAAREPGYED FYVWEDGIPG DNETRLPPNN WVSVFSGSAW QWHEERQQFY
     LRQFTKGQPD LNYRNPAVVQ AMDEVLLYWL QKGVAGFRID AVIYIYEDEQ LRDEPLSGST
     SDPNSVDYLE HIYTRNLPEC YGLIQHWRQL LDNYTADNPG PVRIMMTEGY ADLSLLMNYY
     EDEDGVQGAH FPFNFDFITE LNANSAAPDF VYFIQRWLTY MPPGHSANWV MGNHDNPRVA
     SRYGVGTVDA MNMLMMTLPG IGITYYGEEL GMVDYRDISW NDTVDQPACD AGLDNYKWVS
     RDPERTPMQW SDEKNAGFST GDSTWLPVHP NYQELNLLTQ QEATYSHYKV YQSLIKLRQS
     RVLRDGSFTA QALNRNVFAI KRELRGQPTL LTVINVSNRT QQVDVSNFID LPNRLTLLVV
     GVCSQHRVSE RLKPAEVKLS PHEGLVIQLK AR
//