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Database: UniProt
Entry: A0A1V6MSG5_9ACTN
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ID   A0A1V6MSG5_9ACTN        Unreviewed;       457 AA.
AC   A0A1V6MSG5;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00017303, ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   ORFNames=BM536_011360 {ECO:0000313|EMBL:OQD55246.1};
OS   Streptomyces phaeoluteigriseus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX   NCBI_TaxID=114686 {ECO:0000313|EMBL:OQD55246.1, ECO:0000313|Proteomes:UP000184286};
RN   [1] {ECO:0000313|Proteomes:UP000184286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 41896 {ECO:0000313|Proteomes:UP000184286};
RA   Schniete J.K., Salih T., Algora Gallardo L., Martinez Fernandez S.,
RA   Herron P.R.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OQD55246.1, ECO:0000313|Proteomes:UP000184286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 41896 {ECO:0000313|EMBL:OQD55246.1,
RC   ECO:0000313|Proteomes:UP000184286};
RA   Salih T.S., Algora Gallardo L., Melo Santos T., Filgueira Martinez S.,
RA   Herron P.R.;
RT   "Draft genome sequence of Streptomyces phaeoluteigriseus type strain
RT   DSM41896.";
RL   Submitted (FEB-2017) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQD55246.1}.
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DR   EMBL; MPOH02000011; OQD55246.1; -; Genomic_DNA.
DR   RefSeq; WP_073492973.1; NZ_MPOH02000011.1.
DR   AlphaFoldDB; A0A1V6MSG5; -.
DR   STRING; 114686.BM536_011360; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000184286; Unassembled WGS sequence.
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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR006048; A-amylase/branching_C.
DR   InterPro; IPR031319; A-amylase_C.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
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   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 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..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..457
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013116599"
FT   DOMAIN          33..370
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   DOMAIN          379..455
FT                   /note="Alpha-amylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00632"
SQ   SEQUENCE   457 AA;  49244 MW;  18226B1B021E2B98 CRC64;
     MARRTLSGAL ALSAAALVMT PSLAQASPPG TKDVTAVLFE WNFASVAKEC TTTLGPAGYG
     YVQVSPPAEH IQGAQWWTSY QPVSYKIAGR LGDRTAFQNM VNTCHAAGVK VVVDTVINHM
     SAGSGTGTGG SSYTKYNYPG LYSSYDFDDC TSQITNYGDR WNVQRCELVG LADLDTGEDY
     VRRTIAGYLN DLLSLGVDGF RIDAAKHIDT ADLANIKSRL TKPNAYWKQE AIHGSGEAVQ
     PSEYTGNGDV QEFRYAYDLK RVFNNENLAY LKNYGEGWGY MNSSVSGVFV DNHDTERNGS
     TLSYKDGATY TLANVFMLAW PYGAPDVNSG YEFSDTDAGP PAGGSVSACW QNGWKCQHAW
     PEIQRMVAFR NATRGESVTN WWDNGGDAIA FGRGSKGYVA INHESGSLSR TYQTSLPAGT
     YCNVQNNTTV TVGSSGQFTA TLGANTALAI HAGKSSC
//
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