ID C7QDT7_CATAD Unreviewed; 742 AA.
AC C7QDT7;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
DE Flags: Precursor;
GN OrderedLocusNames=Caci_5853 {ECO:0000313|EMBL:ACU74711.1};
OS Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL
OS B-24433 / ID139908).
OC Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC Catenulisporaceae; Catenulispora.
OX NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU74711.1, ECO:0000313|Proteomes:UP000000851};
RN [1] {ECO:0000313|EMBL:ACU74711.1, ECO:0000313|Proteomes:UP000000851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908
RC {ECO:0000313|Proteomes:UP000000851};
RX PubMed=21304647; DOI=10.4056/sigs.17259;
RA Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S., Chen F.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Mikhailova N.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chain P.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Ali Z., Tindall B.J., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT 139908).";
RL Stand. Genomic Sci. 1:119-125(2009).
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 -!- 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}.
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DR EMBL; CP001700; ACU74711.1; -; Genomic_DNA.
DR RefSeq; WP_015794440.1; NC_013131.1.
DR AlphaFoldDB; C7QDT7; -.
DR STRING; 479433.Caci_5853; -.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; cai:Caci_5853; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_006462_7_3_11; -.
DR InParanoid; C7QDT7; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000000851; Chromosome.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
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 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; IPR031319; A-amylase_C.
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 InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR10357:SF215; ALPHA-AMYLASE 1; 1.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF00686; CBM_20; 1.
DR Pfam; PF01833; TIG; 1.
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.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..742
FT /note="alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002980876"
FT DOMAIN 639..742
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
SQ SEQUENCE 742 AA; 78541 MW; 13DCE3AB695C03D3 CRC64;
MQRRRRLTLV GTAVSLAAAT AVTAAAAPSS AAPARSAAAL NAAALSSTPV STGDMTNDVI
YQLLTDRFYD GNTGNDNPSS SPNLNDSSHN NWQEYWGGDF AGVSAKMQYL SDLGVGAIWI
SPPVENVNVP VPDSTTGATT AGYHGYWGMD FYTPEPHFGQ WADFDAMVAA AHAKGIKVIM
DWAVNDSNPE DTSNPNYGAG GALKQNGTTL STYDNDPNGY FHHNGGVGDY SNLYDVEYQN
LFNLADLAQE NPAVTNYVQG AVDTWLSHGV DGIRMDAVKH MPGGWLKGYV DHIENSHSVF
MYGEWADPSS APLWSDEVKF ANTDGQSLEN FDLNTAVRDV FASNANMSEL DSELSRQQSS
INWSNDLVDF VDSQDENRFL SINNNTTLLD QATVVNMTVP GIPSVYYGDE QYLHNDTTNS
FGQVGGDPYN RAQMTSFAET SRNFAVTQKL AALRKANPAL RYGSSTQRWL NNDVYVYERK
FYNNTVLVAV NKSKTANYAL TGLNTSLPAG SYNDVLSGAL GGGTLTVSTG TGGNNPTGAY
TLNAGQAAVW SYAAPTASTP EVGNIGPTIG HSGDVVAVTG TNFGTTAGTA TVGGTAAPVK
YWSNTEVDLA IPAGATAGLD QVVLTSSAGT ASNGIAYHVE SGTQVPVTFT VTGTSTSPGD
EIYLSGNDDE LGNWSTDTAT AIGPLLDPNY PTWFSLASVP AGATVQFKFF IKHTDGTVTW
EGGSNHTYTV PASGTGTVTV AW
//
