ID   AMY_THECU      STANDARD;      PRT;   605 AA.
AC   P29750;
DT   01-APR-1993 (Rel. 25, Created)
DT   01-APR-1993 (Rel. 25, Last sequence update)
DT   01-FEB-2005 (Rel. 46, Last annotation update)
DE   Alpha-amylase precursor (EC 3.2.1.1) (1,4-alpha-D-glucan
DE   glucanohydrolase).
GN   Name=tam;
OS   Thermomonospora curvata.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptosporangineae; Thermomonosporaceae; Thermomonospora.
OX   NCBI_TaxID=2020;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCM 3352;
RX   MEDLINE=92201705; PubMed=1551601; DOI=10.1016/0378-1119(92)90305-9;
RA   Petricek M., Tichy P., Kuncova M.;
RT   "Characterization of the alpha-amylase-encoding gene from
RT   Thermomonospora curvata.";
RL   Gene 112:77-83(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=92097546; PubMed=1756733;
RA   Marcey D., Watkins W.S., Hazelrigg T.;
RT   "The temporal and spatial distribution pattern of maternal exuperantia
RT   protein: evidence for a role in establishment but not maintenance of
RT   bicoid mRNA localization.";
RL   EMBO J. 10:4259-4266(1991).
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of 1,4-alpha-glucosidic
CC       linkages in oligosaccharides and polysaccharides.
CC   -!- COFACTOR: Binds 1 calcium ion per subunit (By similarity).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Optimum temperature is 65 degrees Celsius;
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- INDUCTION: By maltose or maltodextrins, even in the presence of
CC       glucose.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; X59159; CAA41881.1; -.
DR   PIR; JH0638; JH0638.
DR   HSSP; P29957; 1B0I.
DR   InterPro; IPR006589; Alp_amyl_cat_sub.
DR   InterPro; IPR006048; Alpha_amyl_C.
DR   InterPro; IPR006047; Alpha_amyl_cat.
DR   InterPro; IPR006046; Glyco_hydro_13.
DR   InterPro; IPR002044; Glyco_hydro_CBD.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02806; Alpha-amylase_C; 1.
DR   Pfam; PF00686; CBM_20; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   ProDom; PD001568; Glyco_hydro_CBD; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
KW   Calcium-binding; Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Signal.
FT   SIGNAL        1     33       Potential.
FT   CHAIN        34    605       Alpha-amylase.
FT   ACT_SITE    219    219       Nucleophile (By similarity).
FT   ACT_SITE    253    253       Proton donor (By similarity).
FT   ACT_SITE    313    313       By similarity.
FT   METAL       130    130       Calcium (By similarity).
FT   METAL       189    189       Calcium (By similarity).
FT   METAL       223    223       Calcium (via carbonyl oxygen) (By
FT                                similarity).
SQ   SEQUENCE   605 AA;  64735 MW;  80ABB8F08A69B69A CRC64;
     MGVRRSLAAL LAALLGCATS LVALTVAASP AHAAPSGNRD VIVHLFQWRW KSIADECRTT
     LGPHGFGAVQ VSPPQEHVVL PAEDYPWWQD YQPVSYKLDQ TRRGSRADFI DMVNTCREAG
     VKIYVDAVIN HMTGTGSAGA GPGSAGSSYS KYDYPGIYQS QDFNDCRRDI TNWNDKWEVQ
     HCELVGLADL KTSSPYVQDR IAAYLNELID LGVAGFRIDA AKHIPEGDLQ AILSRLKNVH
     PAWGGGKPYI FQEVIADSTI STGSYTHLGS VTEFQYHRDI SHAFANGNIA HLTGLGSGLT
     PSDKAVVFVV NHDTQRYEPI LTHTDRARYD LAQKFMLAHP YGTPKVMSSY TWSGDDKAGP
     PMHSDGTTRP TDCSADRWLC EHRAVAGMVG FHNAVAGQGI GSAVTDGNGR LAFARGSAGY
     AAFNATNTAW TRTFTTSLPD GVYCDVANGT FVDGVCDGPS YQVSGGKFTA TVPANGAVAL
     HVEAPGSCGP DGCGTPPGGG DDCTTVTARF HATVTTWYGQ EVAVVGSIPE LGSWQPAQGV
     RLRTDSGTYP VWSGAVDLPA GVGFEYKYVK LNRTAPWSGS RAATASPPWM TSGGGCSQNF
     YDSWR
//