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P07191

- MAL2_DROME

UniProt

P07191 - MAL2_DROME

Protein

Maltase A2

Gene

Mal-A2

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 120 (01 Oct 2014)
      Sequence version 2 (05 Jul 2005)
      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 sitei226 – 2261NucleophileBy similarity
    Active sitei298 – 2981Proton donorBy similarity
    Sitei364 – 3641Transition 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 A2 (EC:3.2.1.20)
    Alternative name(s):
    Larval visceral protein D
    Gene namesi
    Name:Mal-A2
    Synonyms:LvpD
    ORF Names:CG8694
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0002569. Mal-A2.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 567544Maltase A2PRO_0000001446Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi30 – 301N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi124 – 1241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi198 – 1981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi312 – 3121N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiP07191.

    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

    BgeeiP07191.

    Interactioni

    Protein-protein interaction databases

    BioGridi61677. 5 interactions.
    MINTiMINT-851985.
    STRINGi7227.FBpp0087826.

    Structurei

    3D structure databases

    ProteinModelPortaliP07191.
    SMRiP07191. Positions 22-562.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 13 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG0366.
    GeneTreeiENSGT00530000063127.
    InParanoidiP07191.
    KOiK01187.
    OMAiDAVPHIY.
    OrthoDBiEOG7B31NK.
    PhylomeDBiP07191.

    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.

    P07191-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPKWAHLGLA ALLLISTTQE GTADIDWWEN ASLYQIYPRS FQDSDGDGIG    50
    DLKGITSRLG YLKEIGITAT WLSPIFTSPM SDFGYDISNF YDIDPIFGTL 100
    EDFDDLIVEA KSLGVKIILD FVPNHSSDEN VWFEKSVNRE DGYDDFYVWD 150
    DGKLNEETGA RDPPSNWVSV FSGPMWTWNE KRQQYFLHQF QVKQPDLNFT 200
    NPMVREHMLD VLKFWLDRGV DGFRIDAVPH IYEHRNADGS YPDEPVSGWG 250
    SDPNAYDYHD HIYTKDQPAT VDLMYEWREF LDNYRAQNGG DSRVLLAEAY 300
    SSVETLSAYF GNSTHQGTQL PMNFQLMYLS GYSTAKDVVG SIDYWMNTMW 350
    KEHQTANWVV GNHDTNRVAD RMGAHKVDLL NVIVNALPGA SVTYYGEEIG 400
    MSNVDVECTG DSCEDRDGER TPMQWTAGKN ADFSDGESTW LPLSPEYQRY 450
    NVQTERGVSR SSLNIFKGLQ ELKSSSAFLA FKEDGGFSYE AVTEQVLQII 500
    RTNKISEEYR ILVNMGNGME ILDGLAPKTY EYVLATAYST HYSGQKADLS 550
    QRIILMPYEA VVLRWLA 567
    Length:567
    Mass (Da):64,542
    Last modified:July 5, 2005 - v2
    Checksum:i51242BA9F185213D
    GO

    Sequence cautioni

    The sequence CAA23492.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti527 – 5271P → T in CAA23492. (PubMed:6854639)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00204 Genomic DNA. Translation: CAA23492.1. Sequence problems.
    AE013599 Genomic DNA. Translation: AAF59088.1.
    AY071566 mRNA. Translation: AAL49188.1.
    PIRiS08597.
    RefSeqiNP_476625.2. NM_057277.2.
    UniGeneiDm.5267.

    Genome annotation databases

    EnsemblMetazoaiFBtr0088747; FBpp0087826; FBgn0002569.
    GeneIDi35825.
    KEGGidme:Dmel_CG8694.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00204 Genomic DNA. Translation: CAA23492.1 . Sequence problems.
    AE013599 Genomic DNA. Translation: AAF59088.1 .
    AY071566 mRNA. Translation: AAL49188.1 .
    PIRi S08597.
    RefSeqi NP_476625.2. NM_057277.2.
    UniGenei Dm.5267.

    3D structure databases

    ProteinModelPortali P07191.
    SMRi P07191. Positions 22-562.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 61677. 5 interactions.
    MINTi MINT-851985.
    STRINGi 7227.FBpp0087826.

    Protein family/group databases

    CAZyi GH13. Glycoside Hydrolase Family 13.

    Proteomic databases

    PaxDbi P07191.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0088747 ; FBpp0087826 ; FBgn0002569 .
    GeneIDi 35825.
    KEGGi dme:Dmel_CG8694.

    Organism-specific databases

    CTDi 35825.
    FlyBasei FBgn0002569. Mal-A2.

    Phylogenomic databases

    eggNOGi COG0366.
    GeneTreei ENSGT00530000063127.
    InParanoidi P07191.
    KOi K01187.
    OMAi DAVPHIY.
    OrthoDBi EOG7B31NK.
    PhylomeDBi P07191.

    Miscellaneous databases

    GenomeRNAii 35825.
    NextBioi 795392.

    Gene expression databases

    Bgeei P07191.

    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.

    Entry informationi

    Entry nameiMAL2_DROME
    AccessioniPrimary (citable) accession number: P07191
    Secondary accession number(s): Q9V4T7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: July 5, 2005
    Last modified: October 1, 2014
    This is version 120 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