ID   A0A0Q5D2P0_9BURK        Unreviewed;       933 AA.
AC   A0A0Q5D2P0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 47.
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=ASF61_10900 {ECO:0000313|EMBL:KQQ33573.1};
OS   Duganella sp. Leaf126.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Duganella.
OX   NCBI_TaxID=1736266 {ECO:0000313|EMBL:KQQ33573.1, ECO:0000313|Proteomes:UP000051032};
RN   [1] {ECO:0000313|EMBL:KQQ33573.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ33573.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQQ33573.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ33573.1};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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   -!- 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:KQQ33573.1}.
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DR   EMBL; LMNW01000031; KQQ33573.1; -; Genomic_DNA.
DR   RefSeq; WP_056157328.1; NZ_LMNW01000031.1.
DR   AlphaFoldDB; A0A0Q5D2P0; -.
DR   STRING; 1736266.ASF61_10900; -.
DR   OrthoDB; 9800174at2; -.
DR   Proteomes; UP000051032; Unassembled WGS sequence.
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; cd02860; E_set_Pullulanase; 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; 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; 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; PF11852; Pullul_strch_C; 1.
DR   Pfam; PF17967; Pullulanase_N2; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF81296; E set domains; 2.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..933
FT                   /note="pullulanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006246457"
FT   DOMAIN          404..779
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   933 AA;  99942 MW;  E55FCB37890BCB37 CRC64;
     METRLAKLFA GAALALTCAA ASAAPTLADC DGPFATVLHA AAPAAAPSST PAASVGSEAR
     AYWLDRQLLQ WPGADRAGVF KLYYAAGAQL RADPGQRVQG ADGALLLAPS AAPAPDALAR
     RFKFIGQGPL LAVAPADVAR IGALLTGQVL LVREAVDGTV LDATAAQLPG ALDDLYASAV
     QAPDLGVTVG ARSAGFKLWA PTAQAVAVCT YASGTSAAAT LTAMRRDDAT GIWSAQLPGT
     QAGRYYRYLV DVVAPGAGLV RNLVTDPYSV SLTTDSRRSY IADLGAAALK PPGWDSTPVP
     QRVKAQPDMA IYELHVRDFS INDASVSAAN RGKYLAFTET GSNGMRHLAA LSRAGMTDIH
     LLPVYDIATI PEQGCQATLQ DIAALPGLRP DGLAQQAAIG AVKFTDCYNW GYDPYHYSAP
     EGSYARDAAD GAARIVEFRR MVQALHRIGL RVGMDVVYNH TFVAGQDPRS VLDRVVPGYY
     HRLDARGAIE RSTCCDNTAT EHPMMAKLMI DSAALWAVHY KIDSFRFDLM GHQPRAAMEQ
     LQARVNRATG RHINLIGEGW NFGEVADGAR FVQASQLSLN GSGIGTFSDR ARDAMRGGGA
     ADGSAQIASQ QGWINGLVYD PNAVARSAPA PRTRDDLMDA ADMVRVGLAG SLRSYPMQTR
     QGPVKRLEDM AYGGNQPAGY ASAPGETVNY VENHDNQTLF DINVFKLPLD TSTAERAQVQ
     MLGAAINAFS QGVPYFHAGF DILRSKSLDR NSFESGDWFN RLDWTYRDNY FGTGLPPEAD
     NGKDYPLMRP LLAQAQRIKP TPQDIAWSRD AFRDLLAIRA SSTLFRLRTA EDVAQRLRFY
     NTGPQQVPTV IVGHLDGAGY PGARFHALTY VINADKVTQQ VTVTQEQGRR YALHPVHLQA
     GAADRRIAAG ARYDAATGSF TVPPRSAVVF VEP
//