ID   J7L5Q4_NOCAA            Unreviewed;       601 AA.
AC   J7L5Q4;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00017303, ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
GN   Name=tam {ECO:0000313|EMBL:AFR08026.1};
GN   OrderedLocusNames=B005_0150 {ECO:0000313|EMBL:AFR08026.1};
OS   Nocardiopsis alba (strain ATCC BAA-2165 / BE74).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Nocardiopsis.
OX   NCBI_TaxID=1205910 {ECO:0000313|EMBL:AFR08026.1, ECO:0000313|Proteomes:UP000003779};
RN   [1] {ECO:0000313|EMBL:AFR08026.1, ECO:0000313|Proteomes:UP000003779}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2165 / BE74 {ECO:0000313|Proteomes:UP000003779};
RX   PubMed=23105086; DOI=10.1128/JB.01522-12;
RA   Qiao J., Chen L., Li Y., Wang J., Zhang W., Chen S.;
RT   "Whole-Genome Sequence of Nocardiopsis alba Strain ATCC BAA-2165,
RT   Associated with Honeybees.";
RL   J. Bacteriol. 194:6358-6359(2012).
RN   [2] {ECO:0000313|Proteomes:UP000003779}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2165 / BE74 {ECO:0000313|Proteomes:UP000003779};
RA   Qiao J., Chen L., Li Y., Wang J., Zhang W., Chen S.;
RT   "Whole-genome sequence of Nocardiopsis alba strain ATCC BAA-2165 associated
RT   with honeybees.";
RL   Submitted (AUG-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}.
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DR   EMBL; CP003788; AFR08026.1; -; Genomic_DNA.
DR   RefSeq; WP_014910485.1; NC_018524.1.
DR   AlphaFoldDB; J7L5Q4; -.
DR   STRING; 1205910.B005_0150; -.
DR   KEGG; nal:B005_0150; -.
DR   PATRIC; fig|1205910.3.peg.140; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_013336_0_0_11; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000003779; 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: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; cd05467; CBM20; 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; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000003779};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..601
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038585573"
FT   DOMAIN          508..601
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
SQ   SEQUENCE   601 AA;  63876 MW;  9B5330069A177776 CRC64;
     MRTPRLGALA AAVLLGTGLL TAPATAAADA APPSPTPAAA QEAGDTIVHL FQWNWDSVAA
     ECVDFLGPRG YGGVQVSPPQ EHVVVPTAEG GNHPWWQDYQ PVSYRIDNTR RGTAEEFRNM
     VETCADQGVR IYVDAVINHM TGPRENEGPG SAGTDWELYE YPDLFGDGEA SYTYEDFGPC
     YETIENWQDK EEVQNCQLLG LADLNTGDPE VRAQIVRYLN GLVALGVGGF RVDASKHVPE
     DDMGAIIGAL DEVPGFGGAP RVYHEVYGDQ TIPYTAYTPY GQVTNFDHQR NLASSFADGN
     IADLTSMPDF GGLTGDESVV FVDNHDTQRY EPTLTYLDGD RYHLATAFML AHPYGTPVVM
     SSYDFRGNVS EGPPSVGEVD GNPAGWITAD SDCSGSDWVC EHRNETVAGM VSFRNAVEGT
     DLTERLRDGS ARVAFDRGET GFAAFNASGQ AWSLSAPTSL PDGAYDNAAG PGTATVADGR
     VTAAVPAEGA LALHVGGECE EGCDGGGEGP GEPGTLTATV ETRPGQEVHV VGSTPELGSW
     EPANGVRLST DADTYPEWRG NVDIAPDAEW KLVRVDTDGT ADWEPGDNRV GPAAAVTWGR
     G
//