ID O24781_BACSP Unreviewed; 700 AA.
AC O24781;
DT 01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT 01-JAN-1998, sequence version 1.
DT 24-JAN-2024, entry version 106.
DE RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00017303, ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN Name=baa {ECO:0000313|EMBL:BAA22082.1};
OS Bacillus sp.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1409 {ECO:0000313|EMBL:BAA22082.1};
RN [1] {ECO:0000313|EMBL:BAA22082.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=No.195 {ECO:0000313|EMBL:BAA22082.1};
RX PubMed=10947962; DOI=10.1042/0264-6021:3500477;
RA Sumitani J., Tottori T., Kawaguchi T., Arai M.;
RT "New type of starch-binding domain: the direct repeat motif in the C-
RT terminal region of Bacillus sp. no. 195 alpha-amylase contributes to starch
RT binding and raw starch degrading.";
RL Biochem. J. 350:477-484(2000).
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR EMBL; AB006823; BAA22082.1; -; Genomic_DNA.
DR AlphaFoldDB; O24781; -.
DR SMR; O24781; -.
DR CAZy; CBM25; Carbohydrate-Binding Module Family 25.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 2.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR005085; CBM25.
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; PF03423; CBM_25; 2.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SMART; SM01066; CBM_25; 2.
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|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..41
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 42..700
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004157693"
FT DOMAIN 53..400
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 409..494
FT /note="Alpha-amylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00632"
FT DOMAIN 506..582
FT /note="Carbohydrate binding module family 25"
FT /evidence="ECO:0000259|SMART:SM01066"
FT DOMAIN 605..684
FT /note="Carbohydrate binding module family 25"
FT /evidence="ECO:0000259|SMART:SM01066"
SQ SEQUENCE 700 AA; 73569 MW; 1A6F3E9218F88AC0 CRC64;
MPALYQGVIA DVRAKRKRLQ VLAKMVLIAL LGTLLSATAF AAPASAAAPG PKDATAVMFS
WTWNAIAREC TENLGPAGYG YVQTSPPQEH IQGAAWWTHY QPVSYKIESR FGTRAEFKAM
VDTCHAAGVK VIADAVINHM TGQSAGGTGW AGSTFQHYDY PGIYQSQDFH SCRRNIANYQ
DRWEVQECNL VNLADLNTSS SYVQGKIAAY LNDLVSLGVD GLRIDAVKHI AASDMQGILS
KVNDRARLYI VQEVIRANEP IQPEEYTSNG DIHEFAFARK LKEAFNGGTI NWLTTGNGIG
PTWAGFLPNA NAAVFVDNHD TERNGETLTY KDGANYDLAQ IFTLAWNYGS PSIHSGYSFS
NNDAGPALAG NGEVIDPVCG QNGWTCKHAQ TGIENMVGFR TQTYGTAVVN KWDNGSSAIA
FGRGDKGYVA INRGSALTRT FQTSLPAGNY CNVIVGLPNS TGCSAGGVVT VDAAGTFTAT
VDQNSAFALH VGAKAGTQQP GPGAGDMKVY YSTSKGWSDY KIHYRVGTGA WTTAPGAGMT
AACAGWVSYT VPAGSTGATA AFNNGSGTWD NNNTSNYALS GAVSTVNGGV VGHTDPCTES
APAPADTAVV FYSTNKGWSA YNIHYRVGTG AWTTAPGSAM TAACTGWMTA SIPLGGASGI
TAAFNNGAGT WDNNAGADYS VGSGYRQVKD GVVSTGNPCA
//
