IAAT_ELECO
ID IAAT_ELECO Reviewed; 122 AA.
AC P01087;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Alpha-amylase/trypsin inhibitor;
DE Short=RBI;
DE AltName: Full=RATI;
OS Eleusine coracana (Indian finger millet) (Ragi).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Chloridoideae; Cynodonteae; Eleusininae; Eleusine.
OX NCBI_TaxID=4511;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Seed;
RA Campos F.A.P., Richardson M.;
RT "The complete amino acid sequence of the bifunctional alpha-amylase/trypsin
RT inhibitor from seeds of ragi (Indian finger millet, Eleusine coracana
RT Gaertn.).";
RL FEBS Lett. 152:300-304(1983).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RC TISSUE=Seed;
RX PubMed=9687373; DOI=10.1016/s0969-2126(98)00092-6;
RA Strobl S., Maskos K., Wiegand G., Huber R., Gomis-Rueth F.-X.,
RA Glockshuber R.;
RT "A novel strategy for inhibition of alpha-amylases: yellow meal worm alpha-
RT amylase in complex with the Ragi bifunctional inhibitor at 2.5-A
RT resolution.";
RL Structure 6:911-921(1998).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RC TISSUE=Seed;
RX PubMed=10089391; DOI=10.1107/s0907444998006271;
RA Gourinath S., Srinivasan A., Singh T.P.;
RT "Structure of the bifunctional inhibitor of trypsin and alpha-amylase from
RT ragi seeds at 2.9-A resolution.";
RL Acta Crystallogr. D 55:25-30(1999).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND DISULFIDE BONDS.
RC TISSUE=Seed;
RX PubMed=10713515; DOI=10.1107/s0907444999016601;
RA Gourinath S., Alam N., Srinivasan A., Betzel C., Singh T.P.;
RT "Structure of the bifunctional inhibitor of trypsin and alpha-amylase from
RT ragi seeds at 2.2 A resolution.";
RL Acta Crystallogr. D 56:287-293(2000).
RN [5]
RP STRUCTURE BY NMR.
RC TISSUE=Seed;
RX PubMed=7599120; DOI=10.1021/bi00026a009;
RA Strobl S., Muehlhahn P., Bernstein R., Wiltscheck R., Maskos K.,
RA Wunderlich M., Huber R., Glockshuber R., Holak T.A.;
RT "Determination of the three-dimensional structure of the bifunctional
RT alpha-amylase/trypsin inhibitor from ragi seeds by NMR spectroscopy.";
RL Biochemistry 34:8281-8293(1995).
CC -!- FUNCTION: May play a protective role against endo- and exogenous
CC hydrolytic activities in the Ragi seeds.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Seeds.
CC -!- SIMILARITY: Belongs to the protease inhibitor I6 (cereal trypsin/alpha-
CC amylase inhibitor) family. {ECO:0000305}.
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DR PIR; A01326; WIILAI.
DR PDB; 1B1U; X-ray; 2.20 A; A=1-122.
DR PDB; 1BIP; NMR; -; A=1-122.
DR PDB; 1TMQ; X-ray; 2.50 A; B=1-117.
DR PDBsum; 1B1U; -.
DR PDBsum; 1BIP; -.
DR PDBsum; 1TMQ; -.
DR AlphaFoldDB; P01087; -.
DR SMR; P01087; -.
DR MINT; P01087; -.
DR MEROPS; I06.003; -.
DR EvolutionaryTrace; P01087; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0015066; F:alpha-amylase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00261; AAI_SS; 1.
DR Gene3D; 1.10.110.10; -; 1.
DR InterPro; IPR044723; AAI_SS_dom.
DR InterPro; IPR006106; Allergen/soft/tryp_amyl_inhib.
DR InterPro; IPR006105; Allergen/tryp_amyl_inhib_CS.
DR InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR Pfam; PF00234; Tryp_alpha_amyl; 1.
DR PRINTS; PR00808; AMLASEINHBTR.
DR SMART; SM00499; AAI; 1.
DR SUPFAM; SSF47699; SSF47699; 1.
DR PROSITE; PS00426; CEREAL_TRYP_AMYL_INH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alpha-amylase inhibitor; Direct protein sequencing;
KW Disulfide bond; Protease inhibitor; Secreted; Serine protease inhibitor.
FT CHAIN 1..122
FT /note="Alpha-amylase/trypsin inhibitor"
FT /id="PRO_0000070490"
FT DISULFID 6..55
FT /evidence="ECO:0000269|PubMed:10713515,
FT ECO:0007744|PDB:1B1U"
FT DISULFID 20..44
FT /evidence="ECO:0000269|PubMed:10713515,
FT ECO:0007744|PDB:1B1U"
FT DISULFID 29..85
FT /evidence="ECO:0000269|PubMed:10713515,
FT ECO:0007744|PDB:1B1U"
FT DISULFID 45..103
FT /evidence="ECO:0000269|PubMed:10713515,
FT ECO:0007744|PDB:1B1U"
FT DISULFID 57..114
FT /evidence="ECO:0000269|PubMed:10713515,
FT ECO:0007744|PDB:1B1U"
FT VARIANT 25..26
FT /note="ST -> AK"
FT VARIANT 28
FT /note="T -> A"
FT VARIANT 70
FT /note="P -> S"
FT HELIX 2..5
FT /evidence="ECO:0007829|PDB:1TMQ"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:1B1U"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:1B1U"
FT HELIX 19..29
FT /evidence="ECO:0007829|PDB:1B1U"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:1BIP"
FT HELIX 37..50
FT /evidence="ECO:0007829|PDB:1B1U"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:1B1U"
FT HELIX 56..64
FT /evidence="ECO:0007829|PDB:1B1U"
FT HELIX 87..93
FT /evidence="ECO:0007829|PDB:1B1U"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:1B1U"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:1B1U"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1B1U"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:1B1U"
SQ SEQUENCE 122 AA; 13138 MW; C8ED7A01CD470E17 CRC64;
SVGTSCIPGM AIPHNPLDSC RWYVSTRTCG VGPRLATQEM KARCCRQLEA IPAYCRCEAV
RILMDGVVTP SGQHEGRLLQ DLPGCPRQVQ RAFAPKLVTE VECNLATIHG GPFCLSLLGA
GE
