ID A0A1Q6FWU5_9BACT Unreviewed; 475 AA.
AC A0A1Q6FWU5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Alpha-amylase {ECO:0000313|EMBL:OKZ03259.1};
GN ORFNames=BHV65_03875 {ECO:0000313|EMBL:OKZ03259.1};
OS Alistipes sp. 58_9_plus.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=1896970 {ECO:0000313|EMBL:OKZ03259.1, ECO:0000313|Proteomes:UP000186889};
RN [1] {ECO:0000313|EMBL:OKZ03259.1, ECO:0000313|Proteomes:UP000186889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=58_9_plus {ECO:0000313|EMBL:OKZ03259.1};
RX PubMed=27819664; DOI=10.1038/nbt.3704;
RA Brown C.T., Olm M.R., Thomas B.C., Banfield J.F.;
RT "Measurement of bacterial replication rates in microbial communities.";
RL Nat. Biotechnol. 34:1256-1263(2016).
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:OKZ03259.1}.
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DR EMBL; MNQG01000027; OKZ03259.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q6FWU5; -.
DR Proteomes; UP000186889; 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 1..384
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 227
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT ACT_SITE 257
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
SQ SEQUENCE 475 AA; 54154 MW; 85C2012A24B27312 CRC64;
MMQYFEWNLP NDGKLWTQLK EDARHLHDVG VTSVWIPPAY KADEQQDEGY AVYDLYDLGE
FDQKGTVRTK YGTRQELEEA IAALHANGIS VYIDTVMNQK TGADYTEKFM ACEVDPENRE
QVIGAPVEVE GWTGYTFPGR GDKYSPFKWH WYHFSGTDQV YETGKRAIYL IQGEGKKWSE
GVDGENGNYD FLIFNDVDFD HPEVIEEMKR WGAWIAQTLD ADGMRLDALK HIRNTFIGEF
MHSVRASRGK EFYAVGEYWS GDFESLEAYL DAVDHQIDLF DAPLHFKLFT ASQQGRDFDL
RTLLDDTLVR KHPTLAVTFV DNHDSQRGSS LESQVKSWFK PLAYGLILLM KEGYPCIFYG
DYYSMKGEAS PHRAVLDILL DARRSRAFGE QTDYFDHPNT VGFTRAGDEQ HPDSGLALLL
SNGEDGEKVM SVGVTHANET WHEITGSYDD EIVIGDDGKA LFRVHGGKLA VWVKK
//
