ID A0A0D8CMT1_9GAMM Unreviewed; 606 AA.
AC A0A0D8CMT1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
GN ORFNames=SG35_30210 {ECO:0000313|EMBL:KJE37484.1};
OS Thalassomonas actiniarum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Thalassomonas.
OX NCBI_TaxID=485447 {ECO:0000313|EMBL:KJE37484.1};
RN [1] {ECO:0000313|EMBL:KJE37484.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A5K-106 {ECO:0000313|EMBL:KJE37484.1};
RA Olonade I., van Zyl L.J., Tuffin M.I.;
RT "Genome sequence of Japanese sea anemone isolate Thalassomonas
RT actiniarum.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000256|RuleBase:RU361134};
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:KJE37484.1}.
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DR EMBL; JYNI01000093; KJE37484.1; -; Genomic_DNA.
DR RefSeq; WP_044836227.1; NZ_CP059735.1.
DR AlphaFoldDB; A0A0D8CMT1; -.
DR STRING; 485447.SG35_30210; -.
DR PATRIC; fig|485447.4.peg.6849; -.
DR OrthoDB; 9805159at2; -.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11314; AmyAc_arch_bac_plant_AmyA; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR012850; A-amylase_bs_C.
DR InterPro; IPR006046; Alpha_amylase.
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:SF48; ALPHA-AMYLASE ISOZYME 3C; 1.
DR Pfam; PF07821; Alpha-amyl_C2; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00810; Alpha-amyl_C2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134};
KW Lyase {ECO:0000313|EMBL:KJE37484.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..606
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002327437"
FT DOMAIN 32..386
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 355..413
FT /note="Alpha-amylase C-terminal beta-sheet"
FT /evidence="ECO:0000259|SMART:SM00810"
SQ SEQUENCE 606 AA; 66044 MW; 7A5864A9AAADFFE0 CRC64;
MIRKMILAIA VGIAASSAVT QAATEQDKAS SAILLQGFHW HSHKTNWYDT IKNQADSVAG
LGVSHVWFPP VSDAASDEGY LPRQLNVLDS NYGSEQALTQ AIFALKNKGV SAVADVVINH
RVGTLDWADF TNPAWGSWAV TCDDEWPGAT GDCDTGGGYA AARDVNHVNN TVQADIVTWL
NTRLKAVGFE GIRYDYSKGY DPYYAGMYSR EVGSNFCVGE VWTDLHYDNV DAHRQLLMDY
INGTSGECGV FDFTTKGLLN KALENNEYWR LANNGSPAGG IGWWGQKMVT FVDNHDTGPS
ESCGSGQQHW PVPCDKVMQG YAYILTHPGI PTIYWAHAFD WNLYDDIKVL ADIRKQQGLS
STSSVSIQAA QTGLYAAIID DKVAVKIGGS NWSPGGSGWQ LAASGSDYAV WTLGEGNDEK
ERTVVFVFGE TASGQDMFIR GGIDHDYAAN NLGLSCTEAN KLCALPISHN NLRNVTTASW
KNNDNYLDWY GIENGQGAGA EGTAADWTTN AWSSSWGTKM TVAVNGFGEE PLNNYGDHYW
MLDAQMDCSK TVNGWFELKT YISNGPGWEA DVSQAGTPYA SGNHFAQCGK ISVFRRGESS
AEFHDF
//
