ID   AMY_STRLI               Reviewed;         919 AA.
AC   Q05884;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Alpha-amylase;
DE            EC=3.2.1.1;
DE   AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE   Flags: Precursor;
GN   Name=amy;
OS   Streptomyces lividans.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 34-43.
RC   STRAIN=TK24;
RX   PubMed=8424949; DOI=10.1016/0167-4781(93)90063-j;
RA   Tsao L.-S., Lin L.-L., Chen J.-C., Chen J.-H., Hsu W.-H.;
RT   "Cloning and characterization of an alpha-amylase gene from Streptomyces
RT   lividans.";
RL   Biochim. Biophys. Acta 1171:255-262(1993).
RN   [2]
RP   ERRATUM OF PUBMED:8424949.
RX   PubMed=8485150;
RA   Tsao L.-S., Lin L.-L., Chen J.-C., Chen J.-H., Hsu W.-H.;
RL   Biochim. Biophys. Acta 1173:119-119(1993).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC         polysaccharides containing three or more (1->4)-alpha-linked D-
CC         glucose units.; EC=3.2.1.1;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; X70255; CAA49759.1; -; Genomic_DNA.
DR   PIR; S28179; S28179.
DR   AlphaFoldDB; Q05884; -.
DR   SMR; Q05884; -.
DR   CAZy; CBM41; Carbohydrate-Binding Module Family 41.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd10315; CBM41_pullulanase; 2.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   InterPro; IPR006048; A-amylase/branching_C.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR005323; CBM41_pullulanase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02806; Alpha-amylase_C; 1.
DR   Pfam; PF03714; PUD; 2.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF49452; SSF49452; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   Calcium; Carbohydrate metabolism; Direct protein sequencing; Glycosidase;
KW   Hydrolase; Metal-binding; Secreted; Signal.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000269|PubMed:8424949"
FT   CHAIN           34..919
FT                   /note="Alpha-amylase"
FT                   /id="PRO_0000001345"
FT   REGION          704..729
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        706..729
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        312
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        346
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         281
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         316
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   SITE            417
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   919 AA;  100642 MW;  035B59FB80F0BD10 CRC64;
     MPATRRTARV RRVAAVTVTA LAAALLPPLA ARADTPPAPP SDAKLAKTAA RHDLTREQFY
     FSCRTLRQRG RRERPRRLTG TRLTTGYDPT DKGFYQGGDL KGLTEKLDYI KGLGTTSIWM
     APIFKNQPVQ GTGKDASAGY HGYWITDFTQ VDPHFGTNKD LKNLISKAHA KGMKVFFDVI
     TNHTADVVDY EEKSYDYLSK GAFPYLTKDG QPFDDADYAD GERRFPRVDS GSFPRTPTVP
     TAKKNLKVPS WLNDPAMYHN RGDSTWAGES ATYGDFNGLD DLWTERPEVV GGMEKIYQRW
     VEDFAIDGFR IDTVKHVDME FWTQWATALD AYAAKKGRDD FFMFGEVYSA DTSVTAPYVT
     QGRLDSTLDF PFQDAARAYA SQGGSARKLA AVFGDDYKYT TDKANAYEQV TFLGNHDMGR
     IGTFLKQDAP EAGDAELLKK DRLANELMFL SRGNPVIYYG DEQGFTGAGG DKDARQPMFA
     SRTADYLDDD QLGTDRTHAE AAYDTSAPLY RQISALAELR KANPALADGV QTERYAADGA
     GIYAFSRTDA KTGTEYVVAF NNAGTEPSAA FATGSAGMTF RGLYGTDATV KSGADSKVTV
     TVPARSAVVL KAAGRLAAPA AEPTISLHAP DPGATGTVEL SADVAGGQLN RVVFAAQTGD
     GKWRTLGTAD HAPYKVTHTV DADTPAGTAL RYKAVVVDSA GRTASGRLHH RHPARRGGAH
     RRLPGPRGRP LQARRRELRR LGPVRLGRPR RREAHHLARH PPLHRPGRLR AFAYVKLKPG
     ASTVGFLVID KDGNKDVAAD RTIDVTETGE VWIEQGEEQL VTERPEYPAQ DTTKAVLHYK
     RADGNYDGWG LHVWGDAANP TDWAKPLQPV RTDPYGAVFE VPLTDGASSL SYMVHKGDEK
     DLPTDQAWTS RPTATRCGC