ID A0A0E0T9F8_GEOS2 Unreviewed; 511 AA.
AC A0A0E0T9F8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN OrderedLocusNames=GYMC52_0636 {ECO:0000313|EMBL:ADU93127.1};
OS Geobacillus sp. (strain Y412MC52).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=550542 {ECO:0000313|EMBL:ADU93127.1, ECO:0000313|Proteomes:UP000002223};
RN [1] {ECO:0000313|EMBL:ADU93127.1, ECO:0000313|Proteomes:UP000002223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y412MC52 {ECO:0000313|EMBL:ADU93127.1,
RC ECO:0000313|Proteomes:UP000002223};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Munk C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mead D., Woyke T.;
RT "Complete sequence of chromosome of Geobacillus sp. Y412MC52.";
RL Submitted (JAN-2011) 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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR EMBL; CP002442; ADU93127.1; -; Genomic_DNA.
DR RefSeq; WP_013523098.1; NC_014915.1.
DR AlphaFoldDB; A0A0E0T9F8; -.
DR KEGG; gya:GYMC52_0636; -.
DR HOGENOM; CLU_006462_7_3_9; -.
DR Proteomes; UP000002223; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11339; AmyAc_bac_CMD_like_2; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR013777; A-amylase-like.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10357:SF215; ALPHA-AMYLASE 1; 1.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR PIRSF; PIRSF001024; Alph-amyl_fung; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..511
FT /note="alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002372875"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 38..386
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 511 AA; 59816 MW; 80E2B6E356624D31 CRC64;
MGNRLFMLLV LPFLLFYAMP AAAAEKEERT WQDEAIYFIM VDRFNNMDPT NDQNVNVNDP
KGYFGGDLKG VTAKLDYIKE MGFTAIWLTP IFKNMPGGYH GYWIEDFYQV DPHFGTLGDL
KTLVKEAHKR DMKVILDFVA NHVGYNHPWL HDPTKKDWFH PKKEIFDWND QTQLENGWMY
GLPDLAQENP EVKTYLIDVA KWWIKETDID GYRLDTVRHV PKSFWQEFAK EVKSVKKDFF
LLGEVWSDDP RYIAEYGKYG IDGFVDYPLY GAVKQSLARR DASLRPLYDV WEYNKTFYDR
PYLLGSFLDN HDTVRFTKLA IDNRNNPISR IKLAMTYLFT APGIPIMYYG TEIAMNGGQD
PDNRRLMDFR ADPEIIDYLK KIGPLRQQLP SLRRGDFTLL YEKDGMAVWK RQYEDETTVI
AINNTGETQH VHLTNDQLPK NKELRGFLLD DLVRGDDDGY DLVLDRETAE VYKLREKTGI
NIPFIAAIVA VYALFLLFLY LVKKRAKRIH E
//
