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Database: UniProt
Entry: D9Y0J6_9ACTN
LinkDB: D9Y0J6_9ACTN
Original site: D9Y0J6_9ACTN 
ID   D9Y0J6_9ACTN            Unreviewed;       573 AA.
AC   D9Y0J6;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 71.
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=SSRG_05691 {ECO:0000313|EMBL:EFL42887.1};
OS   Streptomyces griseoflavus Tu4000.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=467200 {ECO:0000313|EMBL:EFL42887.1, ECO:0000313|Proteomes:UP000002968};
RN   [1] {ECO:0000313|EMBL:EFL42887.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tu4000 {ECO:0000313|EMBL:EFL42887.1};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., 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.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces griseoflavus strain Tu4000.";
RL   Submitted (FEB-2009) 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}.
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DR   EMBL; GG657758; EFL42887.1; -; Genomic_DNA.
DR   RefSeq; WP_004935213.1; NZ_GG657758.1.
DR   AlphaFoldDB; D9Y0J6; -.
DR   STRING; 467200.SSRG_05691; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_013336_0_0_11; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000002968; 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:2001070; F:starch binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR   CDD; cd05808; CBM20_alpha_amylase; 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; IPR006048; A-amylase/branching_C.
DR   InterPro; IPR031319; A-amylase_C.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR002044; CBM_fam20.
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; PF02806; Alpha-amylase_C; 1.
DR   Pfam; PF00686; CBM_20; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SMART; SM01065; CBM_2; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR   PROSITE; PS51166; CBM20; 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..35
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           36..573
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003132665"
FT   DOMAIN          473..573
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
SQ   SEQUENCE   573 AA;  61345 MW;  00F81B726FAE1AD5 CRC64;
     MHRSTSRARR TTAAALALTA GAAGSLLATA APAQAAPPGD KDVTAVMFEW KFDSVAKACT
     DTLGPAGYGF VQVSPPQEHI QGGQWWTSYQ PVSYRIAGRL GDRGQFKSMV DTCHAAGVKV
     VADSVINHMS AGNGTGTGGS SYTKYDYPGL YSRSDFDNCT SQISNYGDRF NVQECELVGL
     ADLDTGEDHA RGKIAGYLND LLSLGVDGFR IDAAKHMAAG DLADIKSRLS NPDVYWKHEA
     IHGAGEAVSP SEYLGSGDVQ EFRYARDLKR IFTGENLAYL KNFGESWGYM ASDKSNVFVA
     NHDTERGGDT LSYRDGAGYT LAHVFMLAWP YGSPDVHSGY EYTDRDAGPP NGGQVNACYS
     DGWKCQHAWR EISSMVGFRN AARGQAVTDW WDNGGDQIAF GRGSKAYVAL NHEGSSLTRT
     FQTSLPAGDY CDVQSGKGVT VDGSGRFTAT LGAGTALALH AGARNCDGGT VPDPDPVASG
     VSFAVNATTS WGQNIYVTGN RPELGNWNPG SALKLDPAAY PVWKLDVELP EGTSFEYKYI
     RKDASGNVTW ESGANRTATV TATRTALNDT WRN
//
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