ID   E4NAB8_KITSK            Unreviewed;       712 AA.
AC   E4NAB8;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00017303, ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
GN   OrderedLocusNames=KSE_23300 {ECO:0000313|EMBL:BAJ28149.1};
OS   Kitasatospora setae (strain ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304
OS   / NBRC 14216 / KM-6054) (Streptomyces setae).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Kitasatospora.
OX   NCBI_TaxID=452652 {ECO:0000313|EMBL:BAJ28149.1, ECO:0000313|Proteomes:UP000007076};
RN   [1] {ECO:0000313|EMBL:BAJ28149.1, ECO:0000313|Proteomes:UP000007076}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304 / NBRC 14216 /
RC   KM-6054 {ECO:0000313|Proteomes:UP000007076};
RX   PubMed=21059706; DOI=10.1093/dnares/dsq026;
RA   Ichikawa N., Oguchi A., Ikeda H., Ishikawa J., Kitani S., Watanabe Y.,
RA   Nakamura S., Katano Y., Kishi E., Sasagawa M., Ankai A., Fukui S.,
RA   Hashimoto Y., Kamata S., Otoguro M., Tanikawa S., Nihira T., Horinouchi S.,
RA   Ohnishi Y., Hayakawa M., Kuzuyama T., Arisawa A., Nomoto F., Miura H.,
RA   Takahashi Y., Fujita N.;
RT   "Genome sequence of Kitasatospora setae NBRC 14216T: an evolutionary
RT   snapshot of the family Streptomycetaceae.";
RL   DNA Res. 17:393-406(2010).
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; Evidence={ECO:0000256|ARBA:ARBA00000548,
CC         ECO:0000256|RuleBase:RU361134};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR   EMBL; AP010968; BAJ28149.1; -; Genomic_DNA.
DR   AlphaFoldDB; E4NAB8; -.
DR   STRING; 452652.KSE_23300; -.
DR   CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR   CAZy; CBM25; Carbohydrate-Binding Module Family 25.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; ksk:KSE_23300; -.
DR   PATRIC; fig|452652.3.peg.2342; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_013336_3_1_11; -.
DR   Proteomes; UP000007076; Chromosome.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:2001070; F:starch binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR   CDD; cd05808; CBM20_alpha_amylase; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR006048; A-amylase/branching_C.
DR   InterPro; IPR031319; A-amylase_C.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR005085; CBM25.
DR   InterPro; IPR002044; CBM_fam20.
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   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR   PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02806; Alpha-amylase_C; 1.
DR   Pfam; PF00686; CBM_20; 1.
DR   Pfam; PF03423; CBM_25; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SMART; SM01065; CBM_2; 1.
DR   SMART; SM01066; CBM_25; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR   PROSITE; PS51166; CBM20; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007076};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..712
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003186822"
FT   DOMAIN          611..712
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
SQ   SEQUENCE   712 AA;  73132 MW;  1F0B6CD6C11DF81B CRC64;
     MPTSAPTRRR RLAAAGTALA ALGLSVGAGF ALAPTATATP PGGKDVTATL FEWKFDSVAK
     ACTDTLGPKG YGFVEVSPAE EHVQGSQWWT SYQPVSYKIA GRLGDRASFR NMVAACHAAG
     VKVIADAVVN HMSAGSGTGT GGTNYTKYTY PGYYQDQDFH SCRTSISNYG DRSNVQNCEL
     VGLSDLNTGS AYVQQTIADY LSDLLTLGVD GFRIDAAKHI AASDLAAIKS KVSNPNAYWV
     QEVIYGAGEA VQPGEYTGTG DVDEFRSATW LKSAFNGGRI SDLQSWGSGL LGSAQARTFV
     DNWDTERNGS TLTYKYGSAY TLANVFMLAN PYGSPNVYSG YAFSGNDDGP PNGGTVNACY
     QDGWNCTHAW RQVANMVGFR NAVAGTGLTN WWSNGNNAIG FGRGDKGYVA INRESGAITQ
     TFQTSLPAGV YCDVQHGDPV NGGGCTGPTH TVGTDGRFTA TVGAGDAVAL YVGAGGGSAA
     TPTPTPSASA SASASATGTG NSATVFYSTN RNWSAYDLHY APTGGSWTTV PGVAMDAACT
     GWVKKTVALG GATGLTATFN NGNGTWDNNG GNNYPLGAGN VTVKDGAVGS GDPCATASAS
     ASASASPSAT AAPSVGTGAS FAVNATTVVG QNIYVVGDAA ELGGWDTSKA LPLSAAAYPV
     WKLDAALNPG TAIQYKYVRK DAAGNVTWES GANRTATVPA SGKVVLNDTW RG
//