ID A0A261FIK3_9BIFI Unreviewed; 580 AA.
AC A0A261FIK3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=BMYO_1523 {ECO:0000313|EMBL:OZG58982.1};
OS Bifidobacterium myosotis.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1630166 {ECO:0000313|EMBL:OZG58982.1, ECO:0000313|Proteomes:UP000216871};
RN [1] {ECO:0000313|EMBL:OZG58982.1, ECO:0000313|Proteomes:UP000216871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100196 {ECO:0000313|EMBL:OZG58982.1,
RC ECO:0000313|Proteomes:UP000216871};
RX PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA van Sinderen D., Ventura M.;
RT "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT family.";
RL BMC Genomics 18:568-568(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OZG58982.1}.
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DR EMBL; MWWW01000016; OZG58982.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261FIK3; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000216871; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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: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 InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
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 PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..45
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 46..580
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013147851"
FT TRANSMEM 555..575
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 51..413
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 422..502
FT /note="Alpha-amylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00632"
SQ SEQUENCE 580 AA; 61543 MW; 0258FAF7B3A48FDB CRC64;
MRIWAKARGF GGLAGLARKM TAAFASLAAA LASASMLPPA PSAVAAEQRG DVIVIAFQTN
WNSVARECAE TYGPEGVGFV QVSPPQESIT GTQWWTSYQP VSYRLDSKLG TESEFKDMVE
ECRAAGVGVI ADVVINHMAG ADRSGMGVAG SSFDGSGDFP AVPYTAANFH DCIQNVSNYR
DADNVQNCRL TGLQDLDTGQ EYVRGRLAEY MAELLDLGVA GFRVDAVKHI SADDMVAIKS
ELARRTNVDL DDVLFEQEVI GSASEAKEIQ PSNYLRTGKV SEFNVNVRLK EAFDGDINSS
SFGLARIGAS ASWVESDKAA VWVTNWDTER NGSALTYKDG AKYLLANAFL LAYGYGQPHL
YSGYYFGDAD DGAPGATATA VVDMVCPENG DEADGTWQCA QRWTAIRGMI GFHNAVSGTE
VVDWREYGEN VVGFGRGEIG YLAVNNSDAP VTRTFATSMP AGVYCNVYAS GDCSAAVFVK
ADGTFEATLP AGSAVAVYAG ATPDDWSGKR RVNSADPDWF VASAVEMAAA QPTAQADAVM
DGETAEAIEE TSRSAGLSVV VLAAAMLLVA VAARVRRFVS
//
