ID   F2JH53_CELLD            Unreviewed;       776 AA.
AC   F2JH53;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00017303, ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   OrderedLocusNames=Clole_0109 {ECO:0000313|EMBL:ADZ81868.1};
OS   Cellulosilyticum lentocellum (strain ATCC 49066 / DSM 5427 / NCIMB 11756 /
OS   RHM5) (Clostridium lentocellum).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Cellulosilyticaceae;
OC   Cellulosilyticum.
OX   NCBI_TaxID=642492 {ECO:0000313|EMBL:ADZ81868.1, ECO:0000313|Proteomes:UP000008467};
RN   [1] {ECO:0000313|EMBL:ADZ81868.1, ECO:0000313|Proteomes:UP000008467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5
RC   {ECO:0000313|Proteomes:UP000008467};
RX   PubMed=21398547; DOI=10.1128/JB.00239-11;
RG   US DOE Joint Genome Institute;
RA   Miller D.A., Suen G., Bruce D., Copeland A., Cheng J.F., Detter C.,
RA   Goodwin L.A., Han C.S., Hauser L.J., Land M.L., Lapidus A., Lucas S.,
RA   Meincke L., Pitluck S., Tapia R., Teshima H., Woyke T., Fox B.G.,
RA   Angert E.R., Currie C.R.;
RT   "Complete genome sequence of the cellulose-degrading bacterium
RT   Cellulosilyticum lentocellum.";
RL   J. Bacteriol. 193:2357-2358(2011).
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|ARBA:ARBA00000548,
CC         ECO:0000256|RuleBase:RU361134};
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}.
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DR   EMBL; CP002582; ADZ81868.1; -; Genomic_DNA.
DR   RefSeq; WP_013655169.1; NC_015275.1.
DR   AlphaFoldDB; F2JH53; -.
DR   STRING; 642492.Clole_0109; -.
DR   KEGG; cle:Clole_0109; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_013336_4_1_9; -.
DR   Proteomes; UP000008467; Chromosome.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
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:UniProtKB-KW.
DR   CDD; cd11315; AmyAc_bac1_AmyA; 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; 3.
DR   InterPro; IPR031319; A-amylase_C.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR005085; CBM25.
DR   InterPro; IPR031965; CBM26.
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   PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR   PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF16738; CBM26; 2.
DR   Pfam; PF16760; CBM53; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SMART; SM01066; CBM_25; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008467};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..776
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038848746"
FT   DOMAIN          51..391
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   DOMAIN          391..465
FT                   /note="Alpha-amylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00632"
FT   DOMAIN          485..568
FT                   /note="Carbohydrate binding module family 25"
FT                   /evidence="ECO:0000259|SMART:SM01066"
SQ   SEQUENCE   776 AA;  85752 MW;  A8200C6F346AA9DE CRC64;
     MKKKFFTKKL AAFLGALGIA FSVIPTTAFN EAVIYAATQT PNLNNIKTKD GIIIQMHMWS
     FNNIKSKLPE LAAAGYKAVQ VSPIQGCIRG TEWWALYQPT NQAIGNPLGS RDDFKALCSE
     AEKYGIDIIV DAVMNHMANN GKGREDEWSS QVVDEFKNWD YYHHVGQNST PDYKDRYRTT
     QGGIGMPDLN TQHPAIQQKA INFLNDCIAS GADGFRFDAV KHIETNVGED VGKSWAGNYW
     TNVLGNLNNK NNLFIYGEAL DEANSNADNI GGYASFMSVT DHYYGKTLRD AVRNYNLPAA
     QSWDINTLPT GTRVSYVENH DNYEHNESNI TDEQRTFAWG ILAARANVTP MYLSRRTGSI
     GSMGTNDWNN DQVKAVNWFH NAMIGQNEYL RYPNGNTCMQ IDRGTKGIAF VNEGSGFNLN
     NAPTNLASGT YTDKGGSGQS YTVSGGKISG YVPSNRIIVL YDNGGIIIPP TTKAVTCNPE
     TPVVSSQATI TYDASNTVLN GASKVNIHWG YDGWKGAKTE SMTSLGSNKW SFTLTVPSGA
     TSNLDLVFNN GGSTWDNNNS TDYSITITAK VTPPIPANRV AYFDNSTFNW NNVYVYVYDE
     SGSTVKEVAK WPGVPMNSKG NHLYEYTLTT DWTDARVIFN NGNTSAQIPD SGQKGFALTG
     IQIYQNNAWA NYDPIEIPST KTIVYFDNSS YNWSNVYIYV YDEKSTSSIQ EVAKWPGVPM
     KNEGNGIYSY EITQDWANKR VIFNNGSNTQ VPGSGQEGYP ISISNMILQN GIWATK
//