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Database: UniProt/TrEMBL
Entry: A0A0U3MZ15_9BURK
LinkDB: A0A0U3MZ15_9BURK
Original site: A0A0U3MZ15_9BURK 
ID   A0A0U3MZ15_9BURK        Unreviewed;       624 AA.
AC   A0A0U3MZ15;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00017303, ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
DE   Flags: Precursor;
GN   ORFNames=RD2015_699 {ECO:0000313|EMBL:ALV05195.1};
OS   Roseateles depolymerans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Roseateles.
OX   NCBI_TaxID=76731 {ECO:0000313|EMBL:ALV05195.1, ECO:0000313|Proteomes:UP000060699};
RN   [1] {ECO:0000313|EMBL:ALV05195.1, ECO:0000313|Proteomes:UP000060699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 42856 {ECO:0000313|EMBL:ALV05195.1,
RC   ECO:0000313|Proteomes:UP000060699};
RA   Kim K.M.;
RT   "Complete genome of Roseateles depolymerans KCTC 42856.";
RL   Submitted (DEC-2015) 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; CP013729; ALV05195.1; -; Genomic_DNA.
DR   RefSeq; WP_058933710.1; NZ_QUMT01000003.1.
DR   AlphaFoldDB; A0A0U3MZ15; -.
DR   STRING; 76731.RD2015_699; -.
DR   KEGG; rdp:RD2015_699; -.
DR   PATRIC; fig|76731.3.peg.710; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000060699; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000060699};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..624
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006842274"
FT   DOMAIN          514..624
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
FT   REGION          596..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   624 AA;  65771 MW;  96522400CFF894E4 CRC64;
     MPQLPFLSRR LAHALTVTAS AALTVFASPA QALNPNSTSV QMFEWAWPDI ATECTQWLGP
     KGFGGVQISP PGASKNANGW WGVYQPVNYA NLTSRMGTPA QLQSMISACH AAGVRVYADI
     VVNQMADGSG TATDGSTWNA ATLTYPFFSA NDFHANCVIN DADYNSPAGR SNVQNCRLGG
     LPDLATESSY VQGQIVNYLK SLLALGIDGF RIDAAKHMPA SAWTSIMSAV KTAYPKTLQG
     ENIWLTQEII NDGEVDRPSY FPIGTINEFQ FTYAMRDVFR GNNGNSLSSI PGIMGTWGNW
     GGSWGFIQPQ NATVFITNWD TERNGSSLNI NNAAGNDAAN QRYTLANIFM LAQGYAEAQL
     YSGFKFSNTD ADRPTTSPYS GGVPQINVVW DFAHRWTPLA NMVGFRNASI GQPQQNWIVG
     NNGNQVAFSR GNVGFVALNN SGSAWTRSFA TGLAAGTYCN VINGTKNAAG TACTADSVTV
     DASGNASFTV PANNSGSTPA VAIYTGQKVT GGGGGGTGTC AVTFTIANAN TVVGQNLRVV
     GSVSGLGAWA PASGFALTIQ GSGANVPWSG TVTLPAGTAI QYKYVKWNGS NAVWESNQTT
     SSGNREFTSC ASGSQARSDG NFKF
//
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