ID   A0A0X3VGA5_9ACTN        Unreviewed;      1085 AA.
AC   A0A0X3VGA5;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE            EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN   ORFNames=ADL15_00605 {ECO:0000313|EMBL:KUL42416.1};
OS   Actinoplanes awajinensis subsp. mycoplanecinus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=135947 {ECO:0000313|EMBL:KUL42416.1, ECO:0000313|Proteomes:UP000053244};
RN   [1] {ECO:0000313|EMBL:KUL42416.1, ECO:0000313|Proteomes:UP000053244}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-16712 {ECO:0000313|EMBL:KUL42416.1,
RC   ECO:0000313|Proteomes:UP000053244};
RA   Gilbert D.G.;
RL   Submitted (OCT-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|ARBA:ARBA00000548};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC       {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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:KUL42416.1}.
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DR   EMBL; LLZH01000001; KUL42416.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0X3VGA5; -.
DR   OrthoDB; 176168at2; -.
DR   Proteomes; UP000053244; Unassembled WGS sequence.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:2001070; F:starch binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd06595; GH31_u1; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR018905; A-galactase_NEW3.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR002044; CBM_fam20.
DR   InterPro; IPR033403; DUF5110.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
DR   InterPro; IPR000322; Glyco_hydro_31_TIM.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR22762:SF89; ALPHA-XYLOSIDASE; 1.
DR   Pfam; PF00686; CBM_20; 1.
DR   Pfam; PF17137; DUF5110; 1.
DR   Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR   Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR   Pfam; PF10633; NPCBM_assoc; 1.
DR   SMART; SM01065; CBM_2; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 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   Glycosidase {ECO:0000256|RuleBase:RU361185};
KW   Hydrolase {ECO:0000256|RuleBase:RU361185, ECO:0000313|EMBL:KUL42416.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053244};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1085
FT                   /note="alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007055901"
FT   DOMAIN          866..976
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
SQ   SEQUENCE   1085 AA;  115525 MW;  33AB4277339D4C77 CRC64;
     MAVLLAVLLT LAGTPGTALA APRPPDVRGQ SVRVGHLRVQ VLSPTLLRLE YAADDDFEDR
     PTFNAVDRAP GHTPFRATTG RGELQVRTSA VTLHYQLDSG PVTAANTTLD LTVGGRRTSV
     RPAFGAQPGE TLGGWYRGLD YYAGQAGPVD QLSLHPGLLD KQGWYLLDDT ATAVRTGADW
     LAARPARTGT YQDGYLFGYG HDYLRALADL RTLTGPSLLP PEWAFGTWFS KYQAYSESDY
     ENQILPAFKS NRVPLDALVM DTDWKAPNQW AGWNWNTTLF PDPAAFIAHL RSEGVNATLN
     VHAAISGDDP RFGAAQATAK GKLQPSTNSF APNPYRFDWG DPDQAAAFAQ LHQPFEQQGV
     RQWWLDYCCD DSTVSTPGVT PDSWVNELYR RDGDARGLRG FALSRIGASF PSYTTVGASG
     PWAEHRSTVH FTGDTEATFA TLAFAAAMTP AEGASIGQSY VSHDIGSFAG KHLSDDLYLR
     WVQLGAFQPI LRLHSDHGDR LPWEYDDAVS GPAADFLRLR ESLVPYLYTA ARQNHDSGIP
     MARALYLTWP EQAEAYQHDT EYLLGDSLLV APVTTAGLST TAPVWFPPGT WTDFFTGETF
     RGPVTRTVGA SPDHMPVYVR AGGILAQRAG DVNIAGQAKD RLTLTAYPHA SGTTSVYEDG
     GEGLGYRAGQ YARIPVRYTE GRRSALTVGP VTGGYPGAPA SRRYTVAFAG VSRPHLVTAG
     GRPAQWTYDA VRHLLTVTVP STASGRAVTV EHDGAVLTVG QRPAVAATFT APDGLQSGAT
     STVVTTATNH GPGTITDVSA TTTVPAGWVI TPRTPTTAAS LAPGATFTVT YDVTPAGASP
     RTQPATAHVA YRNPDGTAAG VPAALTVPLK PVAVTFRVLA PPGTPPDATL YVPGSIAQLG
     PWDPAKQPMT YRGDGVWEAT VSILDGTDVQ YKYTRGSWDT VEEWGTITGT NNRSVTIDGG
     ITHTMLVDDT STAWGSPGVP DIHQAIRYWR DPLVVATTAT AGAVTVRFER DIQPTGTDYA
     GSVAVTGPSG AVSGAVAETE PGTLVWTPAA PLPAGSYTGI VSQVTSAVSD GVPIQKPYSF
     AFTVS
//