ID K6UM88_9MICO Unreviewed; 740 AA.
AC K6UM88;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN ORFNames=AUCHE_08_01440 {ECO:0000313|EMBL:GAB77901.1};
OS Austwickia chelonae NBRC 105200.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC Austwickia.
OX NCBI_TaxID=1184607 {ECO:0000313|EMBL:GAB77901.1, ECO:0000313|Proteomes:UP000008495};
RN [1] {ECO:0000313|EMBL:GAB77901.1, ECO:0000313|Proteomes:UP000008495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 105200 {ECO:0000313|EMBL:GAB77901.1,
RC ECO:0000313|Proteomes:UP000008495};
RA Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y., Ohji S.,
RA Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Austwickia chelonae NBRC 105200.";
RL Submitted (AUG-2012) 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|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}.
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:GAB77901.1}.
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DR EMBL; BAGZ01000008; GAB77901.1; -; Genomic_DNA.
DR RefSeq; WP_006502653.1; NZ_BAGZ01000008.1.
DR AlphaFoldDB; K6UM88; -.
DR STRING; 100225.SAMN05421595_0412; -.
DR eggNOG; COG0366; Bacteria.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000008495; Unassembled WGS sequence.
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 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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008495};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..740
FT /note="alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039507179"
FT DOMAIN 635..740
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
FT REGION 25..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 740 AA; 80640 MW; 61B042AF73D2770F CRC64;
MPHRRLPHIL ATICLSTTAL TSLATQASPP STTGAAPFTA TPVPVPDTTG HDLTGSVIYQ
VLTDRFVNAD RARDEPPTSP GTTSHDRSNW RLYWGGDFAG ITERIPYLKK LGIGALWISP
PVQNIPVSIP AEPSAMTGYH GYWAMDFFTP DPHFGSWQDF DRMVTTAHAA GIKIVMDWAP
NHTSPANVHD SSYGVNGQLR RAGRTLATYH DDPDGYFHHN GGITDYQDLH QAQYRNLFDL
ADLAQEKAEV TTYLKDAVDT WLAHGVDAIR MDAVKHMPGG WLTGYTDHIQ SRRGTFVFGE
WADAASSPLW KDQVDLANTS GMSLQNFDLN TTLRAAFAEG ASLRNVDATV TRQQHSFTYP
HTLINFVDSQ DIPRFLSINP DSSLLDQATV AAMTLPGIPS IYYGDESYLH NDTTNPFGQV
GGDPYNRPMM THFDTDSRQS AIIQRLSELR RENPALRFGN SAERWLDDDI YVYERRFAGN
TVLVAINKSR TVDRPLTGLR TALPAGPHPD RLGGALGGGT LTVTEQDGHD RPTGEYILRA
GQAAVWSVTA TETDRPHIGN VGPTAGHAGS RTVLTGIGFG HDRGQVVVGG HPATVNSWTP
TQVDLTLPTG ITPGRTTIEI KDAQDRNSNR IPYLVRTGPV TPVTVTVTEA PLGPGDRLLL
TGDVAELGNW SAEPPACRGP MLSPGDNTRT LMVALPAGRS VEFKAVIRRP DGSIVWESGD
NHRYDVPTTA TGHTTVAFRR
//
