ID F0IMT9_STRSA Unreviewed; 488 AA.
AC F0IMT9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Alpha-amylase {ECO:0000313|EMBL:EGD36289.1};
DE EC=3.2.1.1 {ECO:0000313|EMBL:EGD36289.1};
GN Name=amyA {ECO:0000313|EMBL:EGD36289.1};
GN ORFNames=HMPREF9383_1442 {ECO:0000313|EMBL:EGD36289.1};
OS Streptococcus sanguinis SK150.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=888811 {ECO:0000313|EMBL:EGD36289.1, ECO:0000313|Proteomes:UP000003530};
RN [1] {ECO:0000313|EMBL:EGD36289.1, ECO:0000313|Proteomes:UP000003530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK150 {ECO:0000313|EMBL:EGD36289.1,
RC ECO:0000313|Proteomes:UP000003530};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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:EGD36289.1}.
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DR EMBL; AEXY01000016; EGD36289.1; -; Genomic_DNA.
DR AlphaFoldDB; F0IMT9; -.
DR PATRIC; fig|888811.3.peg.1418; -.
DR HOGENOM; CLU_024572_2_0_9; -.
DR Proteomes; UP000003530; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11318; AmyAc_bac_fung_AmyA; 1.
DR Gene3D; 2.40.30.140; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR013776; A-amylase_thermo.
DR InterPro; IPR015237; Alpha-amylase_C_pro.
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; PF09154; Alpha-amy_C_pro; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR PIRSF; PIRSF001021; Alph-amls_thrmst; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR001021-2};
KW Glycosidase {ECO:0000313|EMBL:EGD36289.1};
KW Hydrolase {ECO:0000313|EMBL:EGD36289.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2}.
FT DOMAIN 10..398
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 240
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT ACT_SITE 270
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 192
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 203
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 244
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
SQ SEQUENCE 488 AA; 56398 MW; 5DA437AEB8B42918 CRC64;
MKRKIYMENQ TLMQYFEWYL PDDGQHWNRL AEDAPNLAAK GIRKVWMPPA FKGTGSNDVG
YGVYDLFDLG EFDQKGTVRT KYGLKEEYLR AIEALSQNGI EAIADVVLNH KAAADYKERF
TVVEVDPNDR TKVLSEPFEI KGWTKFVFPG RKKAYNDFEW HWYHFTGTDY DAKNNKSGIF
LIQGDNKGWA DDELVDNENG NYDYLMYADI DFKHPEVIQN LYDWAHWFIE STGVHGFRLD
AVKHIDSFFM KNFIRDITEK YGDDFYVFGE FWNSDEKANN DYLENIDYRF DLVDVKLHHN
LFDASKSGAD YDLRTIFDQT LVKNHPESAV TFVDNHDTQR GQALESTVEE WFKPAAYALI
LLREAGLPCV FYGDYYGISG EFAQESFQEL LDKLLDIRLN LAYGEQTDYF DDANCIGWTR
QGMDDGQPIA VLISNGQAAS KSMLVGPEWA GREFSDYLGN NSQIVTIDDQ GWGEFPVEEK
SVSVWSVR
//
