APU_THESA
ID APU_THESA Reviewed; 1279 AA.
AC P36905;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Amylopullulanase;
DE AltName: Full=Alpha-amylase/pullulanase;
DE Includes:
DE RecName: Full=Alpha-amylase;
DE EC=3.2.1.1;
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE Includes:
DE RecName: Full=Pullulanase;
DE EC=3.2.1.41;
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE AltName: Full=Alpha-dextrin endo-1,6-alpha-glucosidase;
DE Flags: Precursor;
GN Name=apu;
OS Thermoanaerobacterium saccharolyticum.
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family III. Incertae Sedis; Thermoanaerobacterium.
OX NCBI_TaxID=28896;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 49915 / DSM 7060 / B6A-RI;
RX PubMed=8117096; DOI=10.1128/aem.60.1.94-101.1994;
RA Ramesh M.V., Podkovyrov S.M., Lowe S.E., Zeikus J.G.;
RT "Cloning and sequencing of the Thermoanaerobacterium saccharolyticum B6A-RI
RT apu gene and purification and characterization of the amylopullulanase from
RT Escherichia coli.";
RL Appl. Environ. Microbiol. 60:94-101(1994).
RN [2]
RP IDENTIFICATION OF PROBABLE VECTOR CONTAMINATION.
RA Robison K.;
RL Unpublished observations (NOV-1994).
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;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages in pullulan,
CC amylopectin and glycogen, and in the alpha- and beta-limit dextrins
CC of amylopectin and glycogen.; EC=3.2.1.41;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q60053};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA19800.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Vector contamination at the C-terminus, a segment of 9 residues, which seems to originate from a puc-type vector.; Evidence={ECO:0000305};
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DR EMBL; L07762; AAA19800.1; ALT_SEQ; Unassigned_DNA.
DR AlphaFoldDB; P36905; -.
DR SMR; P36905; -.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR CAZy; CBM34; Carbohydrate-Binding Module Family 34.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; P36905; -.
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:0051060; F:pullulanase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd02857; E_set_CDase_PDE_N; 1.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 5.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR004185; Glyco_hydro_13_lg-like_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 Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02903; Alpha-amylase_N; 1.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SMART; SM00060; FN3; 2.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50853; FN3; 2.
PE 3: Inferred from homology;
KW Calcium; Carbohydrate metabolism; Glycosidase; Hydrolase; Metal-binding;
KW Repeat; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..1279
FT /note="Amylopullulanase"
FT /id="PRO_0000001324"
FT DOMAIN 930..1022
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1158..1252
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT ACT_SITE 629
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q60053"
FT ACT_SITE 658
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q60053"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q60053"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q60053"
FT BINDING 288
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q60053"
FT BINDING 343
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q60053"
FT BINDING 401
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q60053"
FT BINDING 403
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q60053"
FT BINDING 406
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q60053"
FT BINDING 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q60053"
FT BINDING 452
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q60053"
FT BINDING 454
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q60053"
FT BINDING 527
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P38940"
FT BINDING 627
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P38940"
FT BINDING 734..735
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P38940"
FT BINDING 794
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P38940"
FT BINDING 798
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P38940"
FT SITE 735
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1279 AA; 142431 MW; 095CCBCA391624DD CRC64;
MYKKLFTKKF ISFVMSLLLV LTAAFSSMPF HNVYAADNAS VVANIVGDFQ DQLGDSNWNI
DSNITIMQYV GNGLYEFTTP TQLKAGSYQY KVALNHSWNG GGVPSQGNLT LNLTNDSYVT
FWFDYNTQSV TDSTKYTPIS NDKLPRLVGT IQSAIGAGKD WDPGTSTAIM IDDNFDNVYS
YTAHIPKGDY QYKVTLGNTW AENYGANGVQ DGSNIQLSVA NDADITFFYD ANTHNIWTNY
SPTLTGLDNN IYYDDLKHDT HDPFFRNPFG AIKVGQTVTL RIQAKNHDLE SARISYWDDI
NKTRTELPMT RIGESPDGNY EYWEIKLSFD HPTRIWYYFI LKDGTKTAYY GDNDDQLGGL
GKATDTVNKD FELTVYDKNF DTNDWMKGAV MYQIFPDRFY NGDTSNDHAK TLSRGNDPIE
FHNDWNDLPD NPNNAGTPGY TGDGIWSNDF FGGDLKGIDD KLDYLKGLGV SVIYLNPIFE
SPSNHKYDTA DYTKIDEMFG TTQDFEKLMS DAHAKGINII LDGVFNHTSD DSIYFNRYGK
YPDLGAYQDW KDGNQSLSPY GDWYTINSDG TYECWWGYDS LPVIKSLNGS EYNVTSWANF
IINDKNAISK YWLNPDENLN DGADGWRLDV ENEVAHDFWT HFRDAINTVK PEAPMIAENW
GDASLDLLGD SFNSVMNYQF RNDIIDFLIG QSFDDGNGQH NPIDAAKLDQ RLMSIYERYP
LPAFYSTMNL LGSHDTMSIL TVFGYNSADP NENSDAAKRL AEQKLKLATI LQMGYPGMAD
IYYGDEAGVS GGKDPDDRRT FPWGNEDTAL QDFFKNVSSI RNNNQVLKTG DLETLYAQND
VYAIGRRIIN GKDAFGNSYP DSAAIVAINR SNSDQQITID TTKFLRDGVA FKDLINGDKS
YTINGGQITI NIPAMSGVML ISDDGQDLTA PQVPSNVVAT SGNGKVDLSW SQSDGATGYN
IYRSSVEGGL YEKIASNVTG TTFEDTNVTN GLKYVYAISA VDELGNESEM SIDTVAYPAY
PIGWVGNLTQ VVDNHVISVS NPTEDIYAEV WADGLTNSTG QGPNMIAQLG YKYVGGTVND
SVYGSVYNSV YGVDDSDFTW VNAQYVGDIG NNDQYKASLH LINRSMGYLM RFSDNQGQSW
TTTDTLSFYV VPSDDLIKPT APILNQPGVE SSRVSLTWSP STDNVGIYNY EIYRSDGGTF
NKIATVSNEV YNYVDTSVIN GTTYSYKVVA ADPSFNRTES NVVTIKPDVV PIKVTFNVTV
PDYTPNSVNL AGTFPNATW
