ID   A0A402ATP8_9CHLR        Unreviewed;       869 AA.
AC   A0A402ATP8;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
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   Name=pulA_1 {ECO:0000313|EMBL:GCE22536.1};
GN   ORFNames=KDK_63360 {ECO:0000313|EMBL:GCE22536.1};
OS   Dictyobacter kobayashii.
OC   Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC   Dictyobacteraceae; Dictyobacter.
OX   NCBI_TaxID=2014872 {ECO:0000313|EMBL:GCE22536.1, ECO:0000313|Proteomes:UP000287188};
RN   [1] {ECO:0000313|Proteomes:UP000287188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Uno11 {ECO:0000313|Proteomes:UP000287188};
RA   Wang C.M., Zheng Y., Sakai Y., Toyoda A., Minakuchi Y., Abe K., Yokota A.,
RA   Yabe S.;
RT   "Tengunoibacter tsumagoiensis gen. nov., sp. nov., Dictyobacter kobayashii
RT   sp. nov., D. alpinus sp. nov., and D. joshuensis sp. nov. and description
RT   of Dictyobacteraceae fam. nov. within the order Ktedonobacterales isolated
RT   from Tengu-no-mugimeshi.";
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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:GCE22536.1}.
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DR   EMBL; BIFS01000002; GCE22536.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A402ATP8; -.
DR   Proteomes; UP000287188; 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   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; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000287188}.
FT   DOMAIN          384..771
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   869 AA;  94916 MW;  DDF7A077DA6FDE8B CRC64;
     MISGKEGFQV KKAWKVSLMV LLLLLIGGAG LTQTVRARAA SSVPNVSVKV HYFRPDGMYS
     SWNLWMWTVD TTGAGHNGAS YNFNGTDAYG AVADLSIPAD TGQTAATAQV GFIVREGDWV
     AKDIDTNRFI NIAQGSGEVW LVSGDPTVYT SLDAALEGKK PRVANAFLED NQTVVAKLTT
     PVNFPYAPGD VTVTDTTTNK QLPVKSIVPH DNSSSLQSDL VTITLGVAPD VTHTVELALK
     DVKAATITPR NVLNNSQYTY TGNDMGSQYT PWFTSFRVWA PTASQVNLQL FNSESGALTK
     SVSMHKSEKG TWHLDVLGNL KNWYYLYQVT VQGQTQTAVD PYATGIAVNG TRAMVVDLRT
     TNPAGWNSDH HQTPAHPEDA VIYEVHTRDF TIDANSGVTN KGKFLGFTEQ GTKGPGGVST
     GVDSLKELGV TDVQIMPSYG FASIDETRSD QYNWGYDPRN YNVPEGAYAT DPHGTARITQ
     FKQMVESLHK QGIGVIMDVV YNHTFTTRIS DFDKIVPGYY YRTDFSGSYT NGSGTGNEIA
     AERPMVQKFI RDSVKYWVNE YHVDGFRFDL MALLGVDTMK KISNDLHAIN PGILIHGEPW
     TGGTSALPDS QLLTKGQQKG LKLAVFNDNL RNGLDGNVFD KTAQGFATGA TGLTDVIKKG
     VEGSINDFTA SPRETINYVT SHDNMTLWDK IAASNPNDSV ADRIKMDELA QSVVMTSQGI
     PFMQGGEEML RSKGGNDNSY QAGDAVNEFD WSLKAQHKDV FNFYAGLIEL RKSHPAFRMT
     SAEAIKEHLT FLNSPANTVA FQLKDYANND RWRNIVVVYN PTKAATQLTL PAGQWKVASV
     TEELDTHASA NISGSATVAP ISMEVLYQN
//