ID A0A317L430_9BACI Unreviewed; 691 AA.
AC A0A317L430;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Alpha-amylase {ECO:0000313|EMBL:PWU69658.1};
GN ORFNames=DLJ74_06065 {ECO:0000313|EMBL:PWU69658.1};
OS Gracilibacillus dipsosauri.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Gracilibacillus.
OX NCBI_TaxID=178340 {ECO:0000313|EMBL:PWU69658.1, ECO:0000313|Proteomes:UP000245624};
RN [1] {ECO:0000313|EMBL:PWU69658.1, ECO:0000313|Proteomes:UP000245624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD1 {ECO:0000313|EMBL:PWU69658.1,
RC ECO:0000313|Proteomes:UP000245624};
RA Deutch C.E., Yang S.;
RT "Genomic analysis of Gracilibacillus dipsosauri DD1 reveals novel features
RT of a salt-tolerant amylase.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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:PWU69658.1}.
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DR EMBL; QGTD01000005; PWU69658.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317L430; -.
DR SMR; A0A317L430; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000245624; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11320; AmyAc_AmyMalt_CGTase_like; 1.
DR CDD; cd00604; IPT_CGTD; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR002044; CBM_fam20.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR PANTHER; PTHR10357:SF215; ALPHA-AMYLASE 1; 1.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR Pfam; PF00686; CBM_20; 1.
DR Pfam; PF01833; TIG; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SMART; SM01065; CBM_2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS51166; CBM20; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000245624}.
FT DOMAIN 585..691
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
SQ SEQUENCE 691 AA; 77396 MW; 52E1A6E5BCA46D17 CRC64;
MLLCLLVFQQ FSSEIEASSK VDYSQDVIYQ IVTDRFYDGD PTNNPPGELY SPDASNLHKY
LGGDWQGIIE KIENGYLTDL GVTALWISQP VENVYAVHPE GYTSYHGYWA KDYKKTNPFY
GDLADFQQLV EVAHENGMKI IIDFTPNHSS PALETDPNYV ENGAIYDNGT LLGNYSNDDQ
GLFHHNGGTD FSSLEDGIYR NLYDLADYNL QNETIDQYLK ESIKHWLDLG IDGIRVDAVK
HMSRGWQETL VNHIYTHQPV FTFGEWFLGK GEIDPKNHDF ANESGMSLLD FRYGQALRSV
LKDEDATWTD FHEMIEHTSA SYDEVNDQVT FIDNHDMSRF TSSTTSKTDT EMALAVLLTS
RGVPTIYYGT EQYLTGEGDP ENRKPMPGFD QNTKAYQLIS KLSALRQANP ALGFGNTTER
WINQDVYIYE RKFGDHVVVT AVNSGDTAYN ISNMQTALPS GNYDDVLAGL LNGNSITVNQ
DQQVNSFELV PNEVAVWQYT AESNGPSIGH VGPMVGQQGN DITITGEGFG SSNGNVFFGN
ETAEVKSWSD SEIVVTIPAL AAGKYAVTVE TSSQVSSNNY EGFEILTNQL VPVRFVVDNA
ETDYGTSIYL VGNTQELGNW DVDKAIGPFF NQVMYQYPSW YYDIGVPAGQ EIEFKFIKKD
SQGNVTWESG TNRTYSTPTT GTDTIQFNWR N
//
