APU_THETY
ID APU_THETY Reviewed; 1475 AA.
AC P16950;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 133.
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 Thermoanaerobacter thermohydrosulfuricus (Clostridium
OS thermohydrosulfuricum).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=1516;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=E101-69;
RX PubMed=2391488; DOI=10.1099/00221287-136-3-447;
RA Melasniemi H., Paloheimo M., Hemioe L.;
RT "Nucleotide sequence of the alpha-amylase-pullulanase gene from Clostridium
RT thermohydrosulfuricum.";
RL J. Gen. Microbiol. 136:447-454(1990).
RN [2]
RP PROTEIN SEQUENCE OF 32-39.
RC STRAIN=E101-69;
RX PubMed=3260488; DOI=10.1042/bj2500813;
RA Melasniemi H.;
RT "Purification and some properties of the extracellular alpha-amylase-
RT pullulanase produced by Clostridium thermohydrosulfuricum.";
RL Biochem. J. 250:813-818(1988).
RN [3]
RP DOMAINS FIBRONECTIN TYPE-III.
RX PubMed=1409594; DOI=10.1073/pnas.89.19.8990;
RA Bork P., Doolittle R.F.;
RT "Proposed acquisition of an animal protein domain by bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:8990-8994(1992).
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}.
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DR EMBL; M28471; AAA23205.1; -; Genomic_DNA.
DR PIR; A44765; A44765.
DR AlphaFoldDB; P16950; -.
DR SMR; P16950; -.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR CAZy; CBM34; Carbohydrate-Binding Module Family 34.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
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:2001070; F:starch binding; IEA:InterPro.
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; -; 7.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR002044; CBM_fam20.
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 Pfam; PF00686; CBM_20; 1.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SMART; SM01065; CBM_2; 1.
DR SMART; SM00060; FN3; 2.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49452; SSF49452; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS51166; CBM20; 1.
DR PROSITE; PS50853; FN3; 2.
PE 1: Evidence at protein level;
KW Calcium; Carbohydrate metabolism; Direct protein sequencing; Glycosidase;
KW Hydrolase; Metal-binding; Repeat; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000269|PubMed:3260488"
FT CHAIN 32..1475
FT /note="Amylopullulanase"
FT /id="PRO_0000001323"
FT DOMAIN 928..1019
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1164..1257
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1255..1362
FT /note="CBM20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
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 245
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q60053"
FT BINDING 247
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q60053"
FT BINDING 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q60053"
FT BINDING 340
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q60053"
FT BINDING 398
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q60053"
FT BINDING 400
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 404
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q60053"
FT BINDING 449
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q60053"
FT BINDING 451
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q60053"
FT BINDING 524
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 1475 AA; 165631 MW; 3476C414110BE376 CRC64;
MFKRRALGFL LAFLLVFTAV FGSMPMEFAK AETDTAPAIA NVVGNFQSKL GDSDWNINSD
KTIMTYKGNG FYEFTTPVAL PAGDYEYKVA LNHSWEGGGV PSQGNLSFHL DSDSVVTFYY
NYNTSSITDS TKYTPIPEDK LPRLVGTIQP AIGAGDDWKP ETSTAIMRDY KFNNVYEYTA
NVPKGNYEFK VTLGPSWDIN YGLNGEQNGP NIPLNVAYDT KITFYYDSVS HNIWTDYNPP
LTGPDNNIYY DDLRHDTHDP FFRSPFGAIK TGDTVTLRIQ AKNHDIESAK ISYWDDIKKT
RIEVPMYRIG QSPDGKYEYW EVKLSFDHPT RIWYYFILKD GTKTAYYGDN DEQLGGVGKA
TDTENKDFEL TVYDKNLDTP DWMKGSVMYQ IFPDRFFNGD SSNDHLKKYS RGFDPVEYHS
NWYELPDNPN DKNKLGYTGD GIWSNDFFGG DLKGIDDKLD YLKSLGISVI YLNPIFQSPS
NHRYDTTDYT KIDELLGDLS TFKKLMEDAH AKGIKVILDG VFNHTSDDSI YFDRYGKYLN
TGVLGAYQAW KQGDQSKSPY GDWYEIKPDG TYEGWWGFDS LPVIRQINGS EYNVKSWADF
IINNPNAISK YWLNPDGDKN VGADGWRLDV ANEVAHDFWV HFRGAINTVK PNAPMVAENW
NDASLDLLGD SFNSVMNYLF RNAVIDFILD KSFDDGNVVH NPIDAAKLDQ RLMSIYERYP
LPVFYSTMNL LGSHDTMRIL TVFGYNSADE NQNSQAAKDL AVKRLKLAAI LQMGYPGMPS
IYYGDEAGQS GGKDPDNRRT FPWGREDTDL QTFFKKVVNI RNENQVLKTG DLETLYANGD
VYAFGRRIIN GKDTFGKSYP DSVAIVVINK GDAKQVSIDT TKFIRDGVAF TDALSGKTYT
VQDGKIVVEV GSMDGAILIS DTGQNLTAPQ PITDLKAVSG NGKVDLSWSV VDKAVSYNIY
RSTVKGGLYE KIASNVTQIT YTDTEVTNGL KYVYAVTAVD NDGNESALSN EVEAYPAFPI
GWAGNMNQVN THVIGVNNPV EVYAEVWAQG LTDKPGQGEN MIAQLGYRYI GDTVGDAVYN
AVYNKVEGVE ISKDWTWVDA QYVGDSGNND KYMAKFVPDM VGTWEYIMRF SSNQGHDWTY
TKGPDGKTDE AKQFTVVPSN DVETPTAPVL QQPGIESSRV TLNWSPSADD VAIFGYEIYK
SSSETGPFIK IATVSDSVYN YVDTDVVNGN VYYYKVVAVD TSYNRTASNT VKATPDIIPI
KVTFNVTIPD YTPDDGVNIA GNFPDAFWNP NANQMTKAGS NTYSITLTLN EGTQIEYKYA
RGSWDKVEKG EYGNEIDNRK ITVVNQGSNT MVVNDTVQRW RDVPIYIYSP KDKTIVDANT
SEIEIKGNTY KGAKVTINDE SFVQQENGVF TKVVPLEYGV NTIKIHVEPS GDKNNELTKD
ITITVTREKP ARRQNLLLLH QQKQQNHLKK YHKAK
