ID F9PIJ4_9ACTO Unreviewed; 510 AA.
AC F9PIJ4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Alpha amylase, catalytic domain protein {ECO:0000313|EMBL:EGV14189.1};
GN ORFNames=HMPREF9058_1747 {ECO:0000313|EMBL:EGV14189.1};
OS Actinomyces sp. oral taxon 175 str. F0384.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=944560 {ECO:0000313|EMBL:EGV14189.1, ECO:0000313|Proteomes:UP000004281};
RN [1] {ECO:0000313|EMBL:EGV14189.1, ECO:0000313|Proteomes:UP000004281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0384 {ECO:0000313|EMBL:EGV14189.1,
RC ECO:0000313|Proteomes:UP000004281};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (JUL-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:EGV14189.1}.
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DR EMBL; AFUR01000001; EGV14189.1; -; Genomic_DNA.
DR RefSeq; WP_009406272.1; NZ_AFUR01000001.1.
DR AlphaFoldDB; F9PIJ4; -.
DR eggNOG; COG0366; Bacteria.
DR Proteomes; UP000004281; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; 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; 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 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 Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2}.
FT DOMAIN 19..407
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 246
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT ACT_SITE 276
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT BINDING 119
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 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 314
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 418
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 441
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
SQ SEQUENCE 510 AA; 55894 MW; 4FC8DAB8A99C4378 CRC64;
MTENHAQPSP ANPDDVVNPL LLQAFAWDLP ADSTHWRLLA DNAALLADCG VSSVWLPPAY
KGQAGVEDVG YGVYDTYDLG EFDQKGTVPT KYGTKEDYLA AIEALHAAGI SVVADIVLNH
RMGGDATEVV RATSVDPHDR TCTIGETEEI TAWTRYTFPG RAGAYSDFTW DWTCFHGTDW
DEARRQQGVW LFEGKQWNEN VNDELGNYDY LMGSDVHVID PAVSAEMDRW GRWYVETTGV
DGLRLDALKH VGADFFARWL PELRRATGRA LPAVGEYWSR DVAELEGYLE AVPFMSLFDV
PLHFHLHAAS TSNGDVDLTR LFEGTLVAAD PARAVTFVEN HDTQPGQSLA STIEPWFKPS
AYALILLREA GTPCVFWGDL FGTPETGDLP AVTELPLLMT MRRALAHGPQ HDALDDPDVV
GFAREGDDAH PGSGLAVVLS DRRAATKRLH VGARHAGEQW ICVLGGHEPV TIGDDGNVEL
PVSDGGLSVY APEAARPILD SAEQHLLRQR
//
