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Database: UniProt
Entry: L1KNR1_9ACTN
LinkDB: L1KNR1_9ACTN
Original site: L1KNR1_9ACTN 
ID   L1KNR1_9ACTN            Unreviewed;       461 AA.
AC   L1KNR1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
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=STRIP9103_02455 {ECO:0000313|EMBL:EKX62431.1};
OS   Streptomyces ipomoeae 91-03.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=698759 {ECO:0000313|EMBL:EKX62431.1, ECO:0000313|Proteomes:UP000010411};
RN   [1] {ECO:0000313|EMBL:EKX62431.1, ECO:0000313|Proteomes:UP000010411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91-03 {ECO:0000313|EMBL:EKX62431.1,
RC   ECO:0000313|Proteomes:UP000010411};
RA   Huguet-Tapia J.C., Durkin A.S., Pettis G.S., Badger J.H.;
RL   Submitted (NOV-2012) 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:EKX62431.1}.
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DR   EMBL; AEJC01000517; EKX62431.1; -; Genomic_DNA.
DR   AlphaFoldDB; L1KNR1; -.
DR   PATRIC; fig|698759.3.peg.6869; -.
DR   Proteomes; UP000010411; 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   Reference proteome {ECO:0000313|Proteomes:UP000010411};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..461
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003951678"
FT   DOMAIN          37..374
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   DOMAIN          383..459
FT                   /note="Alpha-amylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00632"
SQ   SEQUENCE   461 AA;  50117 MW;  CE2167B65ACEF6E6 CRC64;
     MISRWTVALT ALTAAAATVM APGAADTAYA SPPGTKDVTA VLFEWRFDSV AKECTNTLGP
     NGYGYVQVSP PAEHIQGSQW WTSYQPVSYK IAGRLGDRTA FQNMVNTCHA AGVKVVVDTV
     INHMSAGSGT GTGGSSYTKY NYPGLYSSFD FDDCTSQISN YQDRWNVQHC ELVGLADLDT
     SEEYVRGAIA RYMNDLLSLG VDGFRVDAAK HMDAADLANI KSRLNNPSVY WKQEVIYGSG
     EAVQPSEYTG NGDVQEFRYA YDLKRVFNNE NLAYLKNYGE GWGYMSSGVS GVFVDNHDTE
     RNGSTLSYKD NANYTLANVF MLAWPYGAPD INSGYEWSDS DAGPPNGGTV NACWQDGWKC
     QHAWPEIMRM VAFRNATRGE SVANWWDNGG DVIAFGRGSK GYVAINHESS SLSRTYQTSL
     PAGTYCNVQN NTTVTVNGSG QFTATLGSNT ALAIYAGKSS C
//
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