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MAL2_DROVI
ID   MAL2_DROVI              Reviewed;         594 AA.
AC   O16099; B4LQJ0;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Maltase 2;
DE            EC=3.2.1.20;
DE   Flags: Precursor;
GN   Name=Mal-B2; Synonyms=Mav2; ORFNames=GJ22506;
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 1-562.
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=AAB82328.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH940649; EDW64447.1; -; Genomic_DNA.
DR   EMBL; AF006573; AAB82328.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_002052292.1; XM_002052256.2.
DR   AlphaFoldDB; O16099; -.
DR   SMR; O16099; -.
DR   STRING; 7244.FBpp0236923; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblMetazoa; FBtr0238431; FBpp0236923; FBgn0022838.
DR   eggNOG; KOG0471; Eukaryota.
DR   HOGENOM; CLU_006462_8_3_1; -.
DR   InParanoid; O16099; -.
DR   OMA; RDWYWWR; -.
DR   OrthoDB; 1384693at2759; -.
DR   PhylomeDB; O16099; -.
DR   Proteomes; UP000008792; Unassembled WGS sequence.
DR   GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   Gene3D; 3.90.400.10; -; 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   Pfam; PF00128; Alpha-amylase; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..594
FT                   /note="Maltase 2"
FT                   /id="PRO_0000001450"
FT   ACT_SITE        241
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        310
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   SITE            377
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        140
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        454
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        537
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        546
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        263
FT                   /note="D -> N (in Ref. 2; AAB82328)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        554..555
FT                   /note="PQ -> L (in Ref. 2; AAB82328)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   594 AA;  67586 MW;  0AB84967886D3785 CRC64;
     MAAAHQLTRT TQLLLLCSLL WTQAPRPVMS SLLSAQTEDF IDWWQHAVFY QIYPRSFKDS
     NGDGIGDLQG VISKLPYLAE TGITATWLSP IFQSPMVDFG YDVSDYKSIQ TEYGTMADFE
     QLVNTATSLG IKIILDFVPN HTSDKHEWFI KSAARDPLYD NFYVWADGKL DNQGVRQPPN
     NWQSVFYGSA WQWHEQRGQY YLHQFAKEQP DLNFRNPAVV RAMDDVLLFW LNKGVAGFRI
     DALNHLFEDE TLPDEPLSGK TTDPLSYDYT KHIYTKDLPE VLSMVQHWRQ LLDDYTAKHS
     EGATRIMMTE AYADLQVLMD YYEDAGGVRG SQLPFNFHFI TDVSGDSDAR DFVYNIEKWL
     IYMPRGHTAN WVMGNHDKPR VATRFGPASV DAMNMLLLTL PGVAVTYNGE ELGMQDYDEI
     SWEDTVDPPA RIAGKLDYKK VSRDPERTPF QWSNATNAGF STAAKTWLPV NPNYLVLNLE
     AQKQAVKSHY KVYKSLIELR KLPVLRRGRF SIEPLSRTVF AFKRTLKDYD TLVTIINVSA
     KEQLVNLTDF INRPQKLVVE VAGVDSVYAP GQTISSSALT LSAHEGLICK LLDA
 
 
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