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