ID   G7VPK1_PAETH            Unreviewed;       692 AA.
AC   G7VPK1;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00017303, ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   OrderedLocusNames=HPL003_21345 {ECO:0000313|EMBL:AET60999.1};
OS   Paenibacillus terrae (strain HPL-003).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=985665 {ECO:0000313|EMBL:AET60999.1, ECO:0000313|Proteomes:UP000005876};
RN   [1] {ECO:0000313|Proteomes:UP000005876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPL-003 {ECO:0000313|Proteomes:UP000005876};
RA   Shin S.H., Kim S., Kim J.Y.;
RT   "Complete sequence of Paenibacillus terrae HPL-003.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HPL-003;
RA   Shin S.H., Kim S., Kim J.Y.;
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AET60999.1, ECO:0000313|Proteomes:UP000005876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPL-003 {ECO:0000313|EMBL:AET60999.1,
RC   ECO:0000313|Proteomes:UP000005876};
RX   PubMed=22328761; DOI=10.1128/JB.06668-11;
RA   Shin S.H., Kim S., Kim J.Y., Song H.Y., Cho S.J., Kim D.R., Lee K.I.,
RA   Lim H.K., Park N.J., Hwang I.T., Yang K.S.;
RT   "Genome Sequence of Paenibacillus terrae HPL-003, a Xylanase-Producing
RT   Bacterium Isolated from Soil Found in Forest Residue.";
RL   J. Bacteriol. 194:1266-1266(2012).
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; CP003107; AET60999.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7VPK1; -.
DR   STRING; 985665.HPL003_21345; -.
DR   KEGG; pta:HPL003_21345; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_013336_4_1_9; -.
DR   Proteomes; UP000005876; 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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd11315; AmyAc_bac1_AmyA; 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; 1.
DR   InterPro; IPR031319; A-amylase_C.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR031965; CBM26.
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   PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR   PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF16738; CBM26; 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..692
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003504570"
FT   DOMAIN          55..393
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   DOMAIN          401..476
FT                   /note="Alpha-amylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00632"
SQ   SEQUENCE   692 AA;  75464 MW;  8B93F0345A0F6312 CRC64;
     MRRTWSIVLF VVLLLQTIGF TPEAQANADV QQLGGSDSKL IAATNYELPE RTKDGLIFHA
     WNWSFANITR NLPELAQAGF KAVQTSPIQA NKEGLTEGSK WWILYQPINF NIGNSQLGSR
     EDFRQLCQEA HKYGISVIVD VVANHTGNAG GGNQQYQPAH NVDPVIKNNR YFWHEARGVE
     NWNDRWQVTQ WGIGLPDLNT SNQELQDIII GFLNDAISLG ADGFRFDAAK HIELPNDPGG
     SNFWPRVLGS LNNKDKLFNY GEVLQGGADN FAGYANYLSL SASSYGDSVR SAVGYHGGIN
     VDAAKFFNAN NVSPSKLVTW VESHDTYAND NSESTGLNDW QIKMGWAIIA SRAETTSLFF
     NRPAGSGKFA NRLGDAGNTL WKDPDIVAVN KFHNAMVGQD EYLRTQGNQI MQVERGTKGM
     TIVNLGGNAQ INSPTRLEEG VYQNKASGGG SFTVSNGRIT GHLDGGKIAV LYNVAQQTPT
     VSVDPGEGPF YTDSVNVRIN YSNANSATYT LNGGPAIPFK SGDMVSIGAG TPIGSTFVLK
     IVAANLSGQT EKTFRYTKEE PSSGITVHFY KPSGWGAPNI YYYDDSVTPL REGSAWPGVA
     MQDEGNGWYV YRAPGWTQAK IIFNSNGNQV PGSQMPGYAV SGEKWIKEGQ FTSQNPQETK
     PTVTIDKPEG AFHGDSLEIT LNTAMPTVVL TD
//