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Database: UniProt
Entry: A0A0X3V8R8_9ACTN
LinkDB: A0A0X3V8R8_9ACTN
Original site: A0A0X3V8R8_9ACTN 
ID   A0A0X3V8R8_9ACTN        Unreviewed;      1063 AA.
AC   A0A0X3V8R8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE            EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN   ORFNames=ADL15_05450 {ECO:0000313|EMBL:KUL41181.1};
OS   Actinoplanes awajinensis subsp. mycoplanecinus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=135947 {ECO:0000313|EMBL:KUL41181.1, ECO:0000313|Proteomes:UP000053244};
RN   [1] {ECO:0000313|EMBL:KUL41181.1, ECO:0000313|Proteomes:UP000053244}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-16712 {ECO:0000313|EMBL:KUL41181.1,
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 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:KUL41181.1}.
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DR   EMBL; LLZH01000017; KUL41181.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0X3V8R8; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000053244; Unassembled WGS sequence.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0051060; F:pullulanase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11341; AmyAc_Pullulanase_LD-like; 1.
DR   CDD; cd10315; CBM41_pullulanase; 2.
DR   CDD; cd02860; E_set_Pullulanase; 1.
DR   Gene3D; 2.60.40.1110; -; 2.
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; 1.
DR   Gene3D; 2.60.40.1130; Rab geranylgeranyltransferase alpha-subunit, insert domain; 1.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR005323; CBM41_pullulanase.
DR   InterPro; IPR004193; Glyco_hydro_13_N.
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; IPR011839; Pullul_strch.
DR   InterPro; IPR024561; Pullul_strch_C.
DR   InterPro; IPR040671; Pullulanase_N2.
DR   NCBIfam; TIGR02103; pullul_strch; 1.
DR   PANTHER; PTHR43002; GLYCOGEN DEBRANCHING ENZYME; 1.
DR   PANTHER; PTHR43002:SF11; PULLULANASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF02922; CBM_48; 1.
DR   Pfam; PF03714; PUD; 2.
DR   Pfam; PF11852; Pullul_strch_C; 1.
DR   Pfam; PF17967; Pullulanase_N2; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF81296; E set domains; 2.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   SUPFAM; SSF49452; Starch-binding domain-like; 2.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053244}.
FT   DOMAIN          11..105
FT                   /note="Pullulanase carbohydrate-binding module 41"
FT                   /evidence="ECO:0000259|Pfam:PF03714"
FT   DOMAIN          118..208
FT                   /note="Pullulanase carbohydrate-binding module 41"
FT                   /evidence="ECO:0000259|Pfam:PF03714"
FT   DOMAIN          253..328
FT                   /note="Pullulanase N2"
FT                   /evidence="ECO:0000259|Pfam:PF17967"
FT   DOMAIN          338..422
FT                   /note="Glycoside hydrolase family 13 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02922"
FT   DOMAIN          900..1060
FT                   /note="Alpha-1,6-glucosidases pullulanase-type C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11852"
SQ   SEQUENCE   1063 AA;  116080 MW;  65AD8A79CC9DFB6E CRC64;
     MLRVTTRPHW LIVHYHRPDG DYSGWALHVW GDVAPDQAAA FPAGQAFDGE DAHGRFAWVR
     LSAEAADVGF VVVHSSGVKD VDLDRRVDVR TTTAILLHAG DRRVHQVPAA PPPDPGFAVL
     HYRRPDGDYS GWGLHVWEGV PIKGKTLWGT PLEPTDFDGY GAVFRVPLKP DAVGLRYVLH
     QSERKDLPDD QRLDLTVTRE VWLLAGTTEP VRPDLGTLGP ELDPARSFAV FVDRTTIALP
     EWFAARAATF ELLTAETTLA LTPRPGGLFQ AQSRRFPHLR AYRAFAVREL GDRVLGGLLR
     DRLLIEGRDT AGDLVARTAV QIAGVLDDLY LEAADADLGL TLDVDRPQLA VWAPTARTVE
     LELSREPGSE PRILPMDRDD LTGVWSIPVK RKWLGRFYRY RVETWHPAAQ RVVTTSVTDP
     YSVSLAADST HSQLVDLDAA ELKPPGWDDA AKPAAVAPAR MQIAEVSVRD FSIGDGSLPA
     AERGTYLAFT HAGSDGMRHL RSLAEAGLTH VHLLPVNDFG TVPDHRADQA QPACDLVTLP
     PDSPEQQRAV MAVADEDGYN WGYDPWHWTT PEGSYATDPA GTARILQMRS AVAALNATGL
     RVVLDVVYNH TMRDGLDRFS VLDRIVPGYY HRLLADGSTA ESTCCPNTAP EHMMMGRLVI
     DSLVTWARAY RIDGFRFDLM GHHPRANILE ARIALDHRVE HGRDICLYGE GWNFGEVAYD
     ARFAQATQVN MAGTGIGSFN DRMRDAARGG GAFGDPGVPG FATGLGQRTP GFVHDRIKVG
     LAGGLATYRF VTHDGVERSG AQVDYNGSPC GYASAPGETV NYVDAHDNEI LYDAMAFKLP
     PGTRPADRAR MQVLALSLVV LGQGAGFMAL GSERLRSKSL DRNSFNSGDW FNQIRWDPGH
     GNGFGTGLPP FDDNREVWGH ARPLLADPAL IPSAEVINLA AERYRELLRI RRSSPVFGLP
     TADEVQRRLT FPLGGPGESP GVIVMGLDGT GLDERWRRLV VVFNATDEPT CQVVPGEGPL
     RLHPELTASV DPVLRGASAV TKLDGAELTV PARQVAVFVA DLA
//
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