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IAMY_COILA
ID   IAMY_COILA              Reviewed;         133 AA.
AC   P15326;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   29-SEP-2021, entry version 93.
DE   RecName: Full=Alpha-amylase inhibitor/endochitinase;
DE            EC=3.2.1.14;
DE   Flags: Fragments;
OS   Coix lacryma-jobi (Job's tears).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Rottboelliinae; Coix.
OX   NCBI_TaxID=4505;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Seed;
RX   PubMed=2605263; DOI=10.1016/0167-4838(89)90007-1;
RA   Ary M.B., Richardson M., Shewry P.R.;
RT   "Purification and characterization of an insect alpha-amylase
RT   inhibitor/endochitinase from seeds of Job's Tears (Coix lachryma-jobi).";
RL   Biochim. Biophys. Acta 999:260-266(1989).
CC   -!- FUNCTION: This protein functions both as an alpha-amylase inhibitor and
CC       as a chitinase.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC         (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC       class I subfamily. {ECO:0000305}.
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DR   CAZy; GH19; Glycoside Hydrolase Family 19.
DR   GO; GO:0015066; F:alpha-amylase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000726; Glyco_hydro_19_cat.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   Pfam; PF00182; Glyco_hydro_19; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
PE   1: Evidence at protein level;
KW   Alpha-amylase inhibitor; Carbohydrate metabolism; Chitin degradation;
KW   Chitin-binding; Direct protein sequencing; Glycosidase; Hydrolase;
KW   Polysaccharide degradation.
FT   CHAIN           <1..>133
FT                   /note="Alpha-amylase inhibitor/endochitinase"
FT                   /id="PRO_0000124818"
FT   ACT_SITE        30
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P29022"
FT   VARIANT         21
FT                   /note="L -> I"
FT   VARIANT         89
FT                   /note="L -> I"
FT   VARIANT         99
FT                   /note="L -> I"
FT   NON_CONS        14..15
FT                   /evidence="ECO:0000305"
FT   NON_CONS        23..24
FT                   /evidence="ECO:0000305"
FT   NON_CONS        32..33
FT                   /evidence="ECO:0000305"
FT   NON_CONS        108..109
FT                   /evidence="ECO:0000305"
FT   NON_CONS        114..115
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         133
SQ   SEQUENCE   133 AA;  14305 MW;  E7E02ED7041B4F5E CRC64;
     CCSKFGYCGL TDAYNFYTGQ LTSFAHVTHE TGNNAYCDPS KTQKPCAAGK KYYGRGPIQI
     SXNYNYGPAG RAIGMDGLGN PDRVAQDALD DYKTALXFLV NGEEAVPGLS AANAVSYYRQ
     YCQQLGVDPG PNL
 
 
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