IAA_STRTE
ID IAA_STRTE Reviewed; 104 AA.
AC P01092;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Alpha-amylase inhibitor HOE-467A;
DE AltName: Full=Tendamistat;
DE Flags: Precursor;
OS Streptomyces tendae.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1932;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31210 / 4158;
RX PubMed=2788646; DOI=10.1128/jb.171.9.4953-4957.1989;
RA Koller K.P., Riess G.;
RT "Heterologous expression of the alpha-amylase inhibitor gene cloned from an
RT amplified genomic sequence of Streptomyces tendae.";
RL J. Bacteriol. 171:4953-4957(1989).
RN [2]
RP PROTEIN SEQUENCE OF 31-104.
RC STRAIN=ATCC 31210 / 4158;
RX PubMed=6605909;
RA Aschauer H., Vertesy L., Nesemann G., Braunitzer G.;
RT "The primary structure of the alpha-amylase inhibitor Hoe 467A from
RT Streptomyces tendae 4158. A new class of inhibitors.";
RL Hoppe-Seyler's Z. Physiol. Chem. 364:1347-1356(1983).
RN [3]
RP CHARACTERIZATION.
RC STRAIN=ATCC 31210 / 4158;
RX PubMed=6611258; DOI=10.1111/j.1432-1033.1984.tb08221.x;
RA Vertesy L., Oeding V., Bender R., Zepf K., Nesemann G.;
RT "Tendamistat (HOE 467), a tight-binding alpha-amylase inhibitor from
RT Streptomyces tendae 4158. Isolation, biochemical properties.";
RL Eur. J. Biochem. 141:505-512(1984).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=3489104; DOI=10.1016/0022-2836(86)90520-6;
RA Pflugrath J.W., Wiegand G., Huber R., Vertesy L.;
RT "Crystal structure determination, refinement and the molecular model of the
RT alpha-amylase inhibitor Hoe-467A.";
RL J. Mol. Biol. 189:383-386(1986).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH ALPHA-AMYLASE.
RX PubMed=7897663; DOI=10.1006/jmbi.1994.0125;
RA Wiegand G., Epp O., Huber R.;
RT "The crystal structure of porcine pancreatic alpha-amylase in complex with
RT the microbial inhibitor Tendamistat.";
RL J. Mol. Biol. 247:99-110(1995).
RN [6]
RP STRUCTURE BY NMR.
RX PubMed=3874968; DOI=10.1016/0022-2836(85)90018-x;
RA Kline A.D., Wuethrich K.;
RT "Secondary structure of the alpha-amylase polypeptide inhibitor tendamistat
RT from Streptomyces tendae determined in solution by 1H nuclear magnetic
RT resonance.";
RL J. Mol. Biol. 183:503-507(1985).
RN [7]
RP STRUCTURE BY NMR.
RX PubMed=3265733; DOI=10.1016/0022-2836(88)90364-6;
RA Kline A.D., Braun W., Wuethrich K.;
RT "Determination of the complete three-dimensional structure of the alpha-
RT amylase inhibitor tendamistat in aqueous solution by nuclear magnetic
RT resonance and distance geometry.";
RL J. Mol. Biol. 204:675-724(1988).
RN [8]
RP STRUCTURE BY NMR.
RX PubMed=2786963; DOI=10.1016/0022-2836(89)90575-5;
RA Billeter M., Kline A.D., Braun W., Huber R., Wuethrich K.;
RT "Comparison of the high-resolution structures of the alpha-amylase
RT inhibitor tendamistat determined by nuclear magnetic resonance in solution
RT and by X-ray diffraction in single crystals.";
RL J. Mol. Biol. 206:677-687(1989).
RN [9]
RP STRUCTURE BY NMR OF MUTANT LEU-49.
RX PubMed=8143730; DOI=10.1111/j.1432-1033.1994.tb18677.x;
RA O'Connell J.F., Bender R., Engels J.W., Koller K.P., Scharf M.,
RA Wuethrich K.;
RT "The nuclear-magnetic-resonance solution structure of the mutant alpha-
RT amylase inhibitor [R19L] Tendamistat and comparison with wild-type
RT Tendamistat.";
RL Eur. J. Biochem. 220:763-770(1994).
CC -!- FUNCTION: Inhibits mammalian alpha-amylases specifically but has no
CC action on plant and microbial alpha-amylases. Forms a tight
CC stoichiometric 1:1 complex with alpha-amylase.
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DR EMBL; M28478; AAA26686.1; -; Genomic_DNA.
DR PIR; A33961; WISMAT.
DR PDB; 1BVN; X-ray; 2.50 A; T=31-104.
DR PDB; 1HOE; X-ray; 2.00 A; A=31-104.
DR PDB; 1OK0; X-ray; 0.93 A; A=31-104.
DR PDB; 2AIT; NMR; -; A=31-104.
DR PDB; 3AIT; NMR; -; A=31-104.
DR PDB; 4AIT; NMR; -; A=31-104.
DR PDBsum; 1BVN; -.
DR PDBsum; 1HOE; -.
DR PDBsum; 1OK0; -.
DR PDBsum; 2AIT; -.
DR PDBsum; 3AIT; -.
DR PDBsum; 4AIT; -.
DR AlphaFoldDB; P01092; -.
DR BMRB; P01092; -.
DR SMR; P01092; -.
DR MINT; P01092; -.
DR EvolutionaryTrace; P01092; -.
DR GO; GO:0015066; F:alpha-amylase inhibitor activity; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.20; -; 1.
DR InterPro; IPR000833; A-amylase_inhib.
DR InterPro; IPR036379; A-amylase_inhib_sf.
DR Pfam; PF01356; A_amylase_inhib; 1.
DR PIRSF; PIRSF001658; Amylase_inhib; 1.
DR SMART; SM00783; A_amylase_inhib; 1.
DR SUPFAM; SSF49498; SSF49498; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alpha-amylase inhibitor; Direct protein sequencing;
KW Disulfide bond; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:6605909"
FT CHAIN 31..104
FT /note="Alpha-amylase inhibitor HOE-467A"
FT /id="PRO_0000014343"
FT DISULFID 41..57
FT /evidence="ECO:0000269|PubMed:6605909"
FT DISULFID 75..103
FT /evidence="ECO:0000269|PubMed:6605909"
FT CONFLICT 59
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:4AIT"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:1OK0"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:1OK0"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1OK0"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:1OK0"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1OK0"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:1OK0"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:2AIT"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:1OK0"
SQ SEQUENCE 104 AA; 10759 MW; 8C58DEF975EA01AE CRC64;
MRVRALRLAA LVGAGAALAL SPLAAGPASA DTTVSEPAPS CVTLYQSWRY SQADNGCAQT
VTVKVVYEDD TEGLCYAVAP GQITTVGDGY IGSHGHARYL ARCL
