ID   D3ICN9_9BACT            Unreviewed;       473 AA.
AC   D3ICN9;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   ORFNames=HMPREF0669_01193 {ECO:0000313|EMBL:EFC70738.1};
OS   Prevotella sp. oral taxon 299 str. F0039.
OG   Plasmid unnamed {ECO:0000313|EMBL:EFC70738.1}.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=575614 {ECO:0000313|EMBL:EFC70738.1, ECO:0000313|Proteomes:UP000015929};
RN   [1] {ECO:0000313|EMBL:EFC70738.1, ECO:0000313|Proteomes:UP000015929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0039 {ECO:0000313|EMBL:EFC70738.1,
RC   ECO:0000313|Proteomes:UP000015929};
RC   PLASMID=unnamed {ECO:0000313|EMBL:EFC70738.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA   Yandava C., Izard J., Baranova O.V., Blanton J.M., Tanner A.C.,
RA   Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EFC70738.1, ECO:0000313|Proteomes:UP000015929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0039 {ECO:0000313|EMBL:EFC70738.1,
RC   ECO:0000313|Proteomes:UP000015929};
RC   PLASMID=Plasmid {ECO:0000313|Proteomes:UP000015929};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Baranova O.V.,
RA   Blanton J.M., Tanner A.C., Dewhirst F.E., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Prevotella sp. Oral Taxon 299 strain F0039.";
RL   Submitted (JUN-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|RuleBase:RU361134};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR   EMBL; CP003667; EFC70738.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3ICN9; -.
DR   KEGG; pro:HMPREF0669_01193; -.
DR   HOGENOM; CLU_013336_4_1_10; -.
DR   OrthoDB; 9806009at2; -.
DR   Proteomes; UP000015929; Plasmid.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
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   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   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
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   Plasmid {ECO:0000313|EMBL:EFC70738.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015929};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..473
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003046564"
FT   DOMAIN          31..392
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   473 AA;  53087 MW;  8AD2AEB5C4EE182A CRC64;
     MIKMKKFFLI MALSCLVLQG IKAHKTVSND EVILHAWCWS FNTIRENLPK IAKAGYTIVQ
     TSPAQHCVTE VKGDKGGGNQ LYGHGKWYYQ YQPTDWKIGN YQMGTRDDLI ALCKEAKRYG
     IRIIVDVLPN HTAVNDCQVE DALDLAVGGH ENLYHANGLT EIKDYNDRLQ CTTGQMGGLP
     DVNTENPDFQ HYYLTYVNDL LSCGVRGFRY DTAKHIGLPS DPKDSKSPEN DFWDVVTGRK
     DVKGLRLALP NDSLFMYGEV LQDANVKEKE YADMIGGVTA STLGWCIRHA LEGHEWKIND
     ITNYCHPVEP QKLITWVESH DTYCNDHESA GLTDSQVRMG WVFITARQFG TPLFYSRPDG
     STLDNVWGNN IVGKKGNDAF LHPEVVAVNK FRKAMHGQKE TIIYANEGKV VEVMRGKKGT
     ALINISSAPQ NISIATMLPN GKYKDVVYQN TFVVSHGILK GTLKPLTSYI LSR
//