ID W4AQ67_9BACL Unreviewed; 792 AA.
AC W4AQ67;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=pullulanase {ECO:0000256|ARBA:ARBA00024062};
DE EC=3.2.1.41 {ECO:0000256|ARBA:ARBA00024062};
DE AltName: Full=Alpha-dextrin endo-1,6-alpha-glucosidase {ECO:0000256|ARBA:ARBA00029618};
DE AltName: Full=Pullulan 6-glucanohydrolase {ECO:0000256|ARBA:ARBA00031076};
GN ORFNames=C169_22545 {ECO:0000313|EMBL:ETT33449.1};
OS Paenibacillus sp. FSL R5-808.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1227076 {ECO:0000313|EMBL:ETT33449.1, ECO:0000313|Proteomes:UP000019053};
RN [1] {ECO:0000313|EMBL:ETT33449.1, ECO:0000313|Proteomes:UP000019053}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-808 {ECO:0000313|EMBL:ETT33449.1,
RC ECO:0000313|Proteomes:UP000019053};
RX PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT "Genomic comparison of sporeforming bacilli isolated from milk.";
RL BMC Genomics 15:26-26(2014).
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 Evidence={ECO:0000256|ARBA:ARBA00023965};
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:ETT33449.1}.
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DR EMBL; ASPT01000043; ETT33449.1; -; Genomic_DNA.
DR AlphaFoldDB; W4AQ67; -.
DR PATRIC; fig|1227076.4.peg.4632; -.
DR Proteomes; UP000019053; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0051060; F:pullulanase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11341; AmyAc_Pullulanase_LD-like; 1.
DR CDD; cd10315; CBM41_pullulanase; 1.
DR CDD; cd02860; E_set_Pullulanase; 1.
DR Gene3D; 2.60.40.1110; -; 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; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR005323; CBM41_pullulanase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
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; IPR049117; pulA_all-beta.
DR InterPro; IPR011840; PulA_typeI.
DR NCBIfam; TIGR02104; pulA_typeI; 1.
DR PANTHER; PTHR43002; GLYCOGEN DEBRANCHING ENZYME; 1.
DR PANTHER; PTHR43002:SF11; PULLULANASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF00128; Alpha-amylase; 2.
DR Pfam; PF02922; CBM_48; 1.
DR Pfam; PF03714; PUD; 1.
DR Pfam; PF21653; pulA_all-beta; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
PE 3: Inferred from homology;
FT DOMAIN 148..578
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 792 AA; 88774 MW; 710CC0A19DC91218 CRC64;
MTVMMSMDMI KSCTSLKLGA IYRREGTAFL VWAPDAVHVS LALYEGAGEY DPQGFVTDHE
GGTLYGMDRN DEGVWSTKVN GDLHGTYYMF KIESTDGTVR YAVDPYATAV SANGSRGAVI
DLAKSNPPGW ELDVRPELLK PTDSVLYELH VRDFSIHADS GMKYRGKYKA FTEGGLRDMG
GNAVGLDHLE ELGVTHVHLL PIFDFRTVNE LDGYATGHLS REYNWGYDPQ NYNVPEGSYA
TDPTDPASRI RELKEMVLAL HSRGIRVVMD VVYNHTYTVD DGPFERLAPG YFYRKDVSGA
LSNGSGVGNE LATEKPMVRK YIKDSLRYWA EEFHIDGFRF DLMALIDTTT MREIVSELRH
EVDNSLLFYG EPWTGGMSPL TEQTVKGSQR DQGFAVFNDH FRHAIKGDND GRGRGFATGE
PWYEGAVVEG MMGSIHDFAL HPSETVNYVT VHDNLNLWDK ILIAEGMEQQ AGLLHLMDGK
LPDGGDVWQA TAASNPYAGV SDEDVMRAVP VRRSLLANGI VLLSQGIPLL HAGDELLRTK
FGDHNSYRSG DAINAIRWSN KQRFRPVFDY YKGLIALRKA HPAFRMTTRE EIEEYMEVLR
SSDRIIAYRL MNSAAGDSWS QIVVVVNGNE HEMTVDLPPT LYRWNIVVNE QHAGTETIET
SDQGAVTVPG LSLMVLYEDR TEMKKGLVTV EVEYERRDQA YDGWNVWVWG TGVQDGSVLF
TQGSSGKARV VFHVASGTKR VGCIVRLNDW EDREGENDWF IDIPPDEVEV RFSLRSGKDE
GFNKKGQRDM AS
//
