ID   A6W7J5_KINRD            Unreviewed;       583 AA.
AC   A6W7J5;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   OrderedLocusNames=Krad_1296 {ECO:0000313|EMBL:ABS02784.1};
OS   Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216).
OC   Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC   Kineococcus.
OX   NCBI_TaxID=266940 {ECO:0000313|EMBL:ABS02784.1, ECO:0000313|Proteomes:UP000001116};
RN   [1] {ECO:0000313|Proteomes:UP000001116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216
RC   {ECO:0000313|Proteomes:UP000001116};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA   Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T.,
RA   Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Bagwell C.E., Shimkets L., Berry C.J.,
RA   Fliermans C., Richardson P.;
RT   "Complete sequence of chromosome of Kineococcus radiotolerans SRS30216.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-maltose = alpha,alpha-trehalose; Xref=Rhea:RHEA:15145,
CC         ChEBI:CHEBI:16551, ChEBI:CHEBI:17306; EC=5.4.99.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00001595};
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. TreS
CC       subfamily. {ECO:0000256|ARBA:ARBA00005496}.
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DR   EMBL; CP000750; ABS02784.1; -; Genomic_DNA.
DR   RefSeq; WP_012084360.1; NC_009664.2.
DR   AlphaFoldDB; A6W7J5; -.
DR   STRING; 266940.Krad_1296; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; kra:Krad_1296; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_006462_2_1_11; -.
DR   OrthoDB; 3203135at2; -.
DR   Proteomes; UP000001116; Chromosome.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0047471; F:maltose alpha-D-glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd11334; AmyAc_TreS; 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   InterPro; IPR032091; Malt_amylase_C.
DR   InterPro; IPR045857; O16G_dom_2.
DR   InterPro; IPR012810; TreS/a-amylase_N.
DR   NCBIfam; TIGR02456; treS_nterm; 1.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF219; MALTOSE ALPHA-D-GLUCOSYLTRANSFERASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF16657; Malt_amylase_C; 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   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001116}.
FT   DOMAIN          28..429
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   583 AA;  65951 MW;  66F6B8EB08716504 CRC64;
     MDLPVPGLQE RGGLRNDPQW YKTAVFYEAL VRAFADSNGS GTGDFSGLTA KLDYLQWLGI
     DCLWLPPFYA SPLRDGGYDI SDYNAVLPEF GTLHDFQRLV TEAHQRGIRI VIDLVMNHTS
     DQHPWFQASR SDPEGPYGDF YVWSDTDEQY PDARIIFVDT ETSNWTFDPV RRQFFWHRFF
     SHQPDLNFDN PAVEEAMFDT VRFWLDMGID GFRLDAVPYL YVREGTNGEN LPETHDYLHR
     LRRMVDEEYP GRVLLAEANQ WPFDVVEYFG TEEAPECHMC FHFPVMPRLY YALREGRATP
     ITEILSATPD IPTSSGQWGT FLRNHDELTL EMVTTEERAA MYGWYAPDPR MRANVGIRRR
     LAPLLDNSRP EIQLIHALVL SLPGSPCLYY GDEIGMGDNI WLDDRDAVRT PMQWTPDRNS
     GFSSADPGKL YLPTIQSLVY HYQSVNVEAQ LATGSSLLHW VRNVLAVRRA HPAFGRGRYL
     PLPTRDDPRP DDGSCSNEAV LAFLRVLDPT PEEEGETVLC LNNLSDHPQA AVLRMPGQAG
     ATARDVFGGA AFGEVDAEGT LTVMLGSRGF YWLALTGGRG VGA
//