ID   A0A120F6Z6_9ACTN        Unreviewed;       732 AA.
AC   A0A120F6Z6;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 41.
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   ORFNames=GA0070623_0852 {ECO:0000313|EMBL:SCG42051.1};
OS   Micromonospora rifamycinica.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=291594 {ECO:0000313|EMBL:SCG42051.1, ECO:0000313|Proteomes:UP000198226};
RN   [1] {ECO:0000313|EMBL:SCG42051.1, ECO:0000313|Proteomes:UP000198226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44983 {ECO:0000313|EMBL:SCG42051.1,
RC   ECO:0000313|Proteomes:UP000198226};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LT607752; SCG42051.1; -; Genomic_DNA.
DR   RefSeq; WP_067315644.1; NZ_LT607752.1.
DR   AlphaFoldDB; A0A120F6Z6; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000198226; Chromosome i.
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; IPR031319; A-amylase_C.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR013784; Carb-bd-like_fold.
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; PF00686; CBM_20; 2.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SMART; SM01065; CBM_2; 2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   SUPFAM; SSF49452; Starch-binding domain-like; 2.
DR   PROSITE; PS51166; CBM20; 2.
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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..732
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039057518"
FT   REGION          507..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          710..732
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   732 AA;  75960 MW;  3B67D69D442EB163 CRC64;
     MSVPRVPRGT RLRRGLLALA VTASSLAALS ALPATAPATA AVALNDSEVT ANLWEWNWRS
     VAAACTDHLG PAGYGAVQVA PPQESVSLPS SADGVHPWYE VYQPVSYRLE SRFGTRQQFA
     DMVTACHNAG VRVYVDAVVN HMAGANNPES VVGYAGTDFS GPGYSFPAVP YGTGDFHRPG
     DNCPTSGAIN DWNNEAQVTS CELLSLTDLY TEKDAVRTKI AGFLNDLVGL GVDGFRVDAV
     KHVKKDDFAA ILGKVRNTTA ENKRPYVAQE IFDGASNDAL KARAFTGNGD VLDFGYAKGL
     KSAFQGSIAN LANVGSWNLD APSANVFAMV TNHDLERDGV VLSYRDGSDY VLANYFALAY
     PHGKPSVYDS FTWSNRNQSP PADGNGYVTD TVCGGSWNCL TRSTGIKGMV GWANTAKSVR
     TVSDFTVVNS NVIGFHRGDR AWIGINDSGS ASTATFTTGL ADGSYCDVIS GARGTAGCTG
     TTVTVSGGRA TVRIPANGAV ALHANAKAGS TPTPTATPTA SPTPTATPTP TAPAGTVATT
     FTVTASLAGG QDAYVVGSVP ALGSWSPADA VRLTAQGGGV YRAVVTLPAA TTVEFKFLKK
     TTAGVVTWES GGNRTLTTPA GGTSSVTDTF RGDPAGTQGA SFTVNATTSY GQNVFVVGSV
     AALGSWNPAN AVALSSAAYP LWRATVALPA NTAFEYKYLK KNPDGTVTWE SGGNRSATVG
     STGSWSANDT WR
//