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P07190

- MAL1_DROME

UniProt

P07190 - MAL1_DROME

Protein

Maltase A1

Gene

Mal-A1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (02 Feb 2004)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei221 – 2211NucleophileBy similarity
    Active sitei297 – 2971Proton donorBy similarity
    Sitei363 – 3631Transition state stabilizerBy similarity

    GO - Molecular functioni

    1. cation binding Source: InterPro
    2. maltose alpha-glucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Protein family/group databases

    CAZyiGH13. Glycoside Hydrolase Family 13.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Maltase A1 (EC:3.2.1.20)
    Alternative name(s):
    Larval visceral protein H
    Gene namesi
    Name:Mal-A1
    Synonyms:LvpH
    ORF Names:CG8696
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0002570. Mal-A1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 577558Maltase A1PRO_0000001447Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi151 – 1511N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi244 – 2441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi315 – 3151N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi331 – 3311N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiP07190.
    PRIDEiP07190.

    Expressioni

    Developmental stagei

    One of the proteins expressed by the 44D cuticle gene cluster. Expressed in first, second and early 3rd instar larvae and in adults, but not in embryos or pupae.1 Publication

    Gene expression databases

    BgeeiP07190.

    Interactioni

    Protein-protein interaction databases

    BioGridi61676. 5 interactions.
    MINTiMINT-1599685.
    STRINGi7227.FBpp0087838.

    Structurei

    3D structure databases

    ProteinModelPortaliP07190.
    SMRiP07190. Positions 19-577.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 13 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG0366.
    GeneTreeiENSGT00530000063127.
    InParanoidiP07190.
    KOiK01187.
    OMAiMMDIVAN.
    OrthoDBiEOG7B31NK.
    PhylomeDBiP07190.

    Family and domain databases

    Gene3Di3.20.20.80. 2 hits.
    InterProiIPR015902. Glyco_hydro_13.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR006589. Glyco_hydro_13_sub_cat_dom.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10357. PTHR10357. 1 hit.
    PfamiPF00128. Alpha-amylase. 1 hit.
    [Graphical view]
    SMARTiSM00642. Aamy. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P07190-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRPQSAACLL LAIVGFVGAT EWWESGNYYQ IYPRSFRDSD GDGIGDLNGV    50
    TEKLQYLKDI GFTGTWLSPI FKSPMVDFGY DISDFYQIHP EYGTMEDFER 100
    MIAKAKEVGI KIILDFVPNH SSTENEWFTK SVDSDPVYKD FYIWHDGKIN 150
    NETGEREPPS NWNSEFRYSA WEWNEVRQQY YLHQFAIQQA DLNYRNPAVV 200
    NEMKNVIRFW LGKGVSGFRI DAVPYLFEVD LDRYNQYPDE PLTNDSVNCP 250
    DPDDHCYTQH IYTQDMPETI DMVYQWRELV DEFHVENGGD KRLLMTEAYT 300
    SFENIMTYYG NGVRNGSHIP FNFDFLTSIN NASKAGEYVE HIKKWMDAMP 350
    EGVYANWVLG NHDNKRVASR FGVQRTDLIN ILLQTLPGHA VTYNGEELGM 400
    TDVWISWEDT VDPNACNSDP DNYYARSRDP ARSPYQWDAS SKAGFTSADH 450
    TWLPVADDYK TNNALQQLRA PRSHLQIFKK LVRVRKEPSF RQGELNIQAI 500
    DDDVIIYSRQ KTGSDLYVIV LNLGSTSKTL DLTKYYELGT QAEVITTSLS 550
    SQYIDGDVIK STEFVANPYV GTVLVAV 577
    Length:577
    Mass (Da):66,386
    Last modified:February 2, 2004 - v2
    Checksum:iE005AE05F98ABE0F
    GO

    Sequence cautioni

    The sequence AAL48097.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00204 Genomic DNA. Translation: CAA23491.1. Sequence problems.
    AE013599 Genomic DNA. Translation: AAF59089.3.
    AY070626 mRNA. Translation: AAL48097.2. Different initiation.
    PIRiS07253.
    RefSeqiNP_476627.3. NM_057279.4.
    UniGeneiDm.1825.

    Genome annotation databases

    EnsemblMetazoaiFBtr0088759; FBpp0087838; FBgn0002570.
    GeneIDi35824.
    KEGGidme:Dmel_CG8696.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00204 Genomic DNA. Translation: CAA23491.1 . Sequence problems.
    AE013599 Genomic DNA. Translation: AAF59089.3 .
    AY070626 mRNA. Translation: AAL48097.2 . Different initiation.
    PIRi S07253.
    RefSeqi NP_476627.3. NM_057279.4.
    UniGenei Dm.1825.

    3D structure databases

    ProteinModelPortali P07190.
    SMRi P07190. Positions 19-577.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 61676. 5 interactions.
    MINTi MINT-1599685.
    STRINGi 7227.FBpp0087838.

    Protein family/group databases

    CAZyi GH13. Glycoside Hydrolase Family 13.

    Proteomic databases

    PaxDbi P07190.
    PRIDEi P07190.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0088759 ; FBpp0087838 ; FBgn0002570 .
    GeneIDi 35824.
    KEGGi dme:Dmel_CG8696.

    Organism-specific databases

    CTDi 35824.
    FlyBasei FBgn0002570. Mal-A1.

    Phylogenomic databases

    eggNOGi COG0366.
    GeneTreei ENSGT00530000063127.
    InParanoidi P07190.
    KOi K01187.
    OMAi MMDIVAN.
    OrthoDBi EOG7B31NK.
    PhylomeDBi P07190.

    Miscellaneous databases

    GenomeRNAii 35824.
    NextBioi 795387.

    Gene expression databases

    Bgeei P07190.

    Family and domain databases

    Gene3Di 3.20.20.80. 2 hits.
    InterProi IPR015902. Glyco_hydro_13.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR006589. Glyco_hydro_13_sub_cat_dom.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR10357. PTHR10357. 1 hit.
    Pfami PF00128. Alpha-amylase. 1 hit.
    [Graphical view ]
    SMARTi SM00642. Aamy. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Two gene families clustered in a small region of the Drosophila genome."
      Snyder M., Davidson N.
      J. Mol. Biol. 166:101-118(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE.
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    5. Cited for: SEQUENCE REVISION.

    Entry informationi

    Entry nameiMAL1_DROME
    AccessioniPrimary (citable) accession number: P07190
    Secondary accession number(s): Q9V4T6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: February 2, 2004
    Last modified: October 1, 2014
    This is version 125 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3