ID A0A1I5X1Z6_9BACT Unreviewed; 493 AA.
AC A0A1I5X1Z6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Alpha-amylase {ECO:0000313|EMBL:SFQ26042.1};
GN ORFNames=SAMN05444277_107156 {ECO:0000313|EMBL:SFQ26042.1};
OS Parafilimonas terrae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Parafilimonas.
OX NCBI_TaxID=1465490 {ECO:0000313|EMBL:SFQ26042.1, ECO:0000313|Proteomes:UP000199031};
RN [1] {ECO:0000313|EMBL:SFQ26042.1, ECO:0000313|Proteomes:UP000199031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28286 {ECO:0000313|EMBL:SFQ26042.1,
RC ECO:0000313|Proteomes:UP000199031};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR EMBL; FOXQ01000007; SFQ26042.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5X1Z6; -.
DR STRING; 1465490.SAMN05444277_107156; -.
DR OrthoDB; 9806009at2; -.
DR Proteomes; UP000199031; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000199031}.
FT DOMAIN 3..394
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 232
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT ACT_SITE 262
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT BINDING 102
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 236
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
SQ SEQUENCE 493 AA; 57122 MW; 9676B6F9365C0F8A CRC64;
MRKTIFQFFH WYYPKGKLWK QVMEQAHHLE WLGISDVWLP PPYKSSAGAD GVGYDVYDLF
DLGEFDQKGS VKTRYGTKKQ FINAVKTLHK HNLGAMGDIV LNHKNGADET ERVNVIKVDY
QDRNKVISEP FEKDINTKYY FPGRNKKYSE FVWDFHAFTG IDECSSDNEK CIYKIINGYG
DLWDDVVGDE FGNFDYLLGA DIEFRNPNVT AELKYWGKWF IETCYIDSLR LDAVKHISAR
FYKEWLDYLK ETFQKDFFTV AEYWSSDLKY LHEYLDVMEN RVQLFDVPLH RNFFDASRQG
KDFNLAGIFN NTLLQTRSQS AVTFVDNHDT QPAQALESFV DYWFKPHANA LILLRQEGIP
CVFHPSYYGA SYNVNGNDIH LAPVPNLYKM LMIRKNLFEG EQHDYFDHPN CISWFVSGTE
QNRNAGFVVV LSNGDDGFKE MNLSGLNGNR KFIDVTGSFA DAVVTNADGA AIFPVKSRSI
SIWIKEEALE SIK
//
