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
//