ID   A0A0P0CXB4_9BACT        Unreviewed;       663 AA.
AC   A0A0P0CXB4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=DC20_12620 {ECO:0000313|EMBL:ALJ01426.1};
OS   Rufibacter tibetensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Rufibacter.
OX   NCBI_TaxID=512763 {ECO:0000313|EMBL:ALJ01426.1, ECO:0000313|Proteomes:UP000061382};
RN   [1] {ECO:0000313|EMBL:ALJ01426.1, ECO:0000313|Proteomes:UP000061382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1351 {ECO:0000313|EMBL:ALJ01426.1,
RC   ECO:0000313|Proteomes:UP000061382};
RA   Dai J.;
RT   "Complete genome sequence of Rufibacter tibetensis strain 1351t, a
RT   radiation-resistant bacterium from tibet plateau.";
RL   Submitted (AUG-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};
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DR   EMBL; CP012643; ALJ01426.1; -; Genomic_DNA.
DR   RefSeq; WP_062545946.1; NZ_CP012643.1.
DR   AlphaFoldDB; A0A0P0CXB4; -.
DR   SMR; A0A0P0CXB4; -.
DR   STRING; 512763.DC20_12620; -.
DR   KEGG; rti:DC20_12620; -.
DR   PATRIC; fig|512763.3.peg.2768; -.
DR   OrthoDB; 9761875at2; -.
DR   Proteomes; UP000061382; Chromosome.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; 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   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; 1.
DR   Pfam; PF02922; CBM_48; 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.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000061382};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..663
FT                   /note="pullulanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006043025"
FT   DOMAIN          189..566
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   663 AA;  75276 MW;  D15E6D78CAB361E3 CRC64;
     MKRRKLLPVL FSFLFLMSSS TTWAQAHKFD QYPTPKQANL WTEYKPEGTT FKLWSPVAEE
     VVVKFYDKGY GGTVREKRSM RKGEKGLWRL VVKKNLQGVY YTYHVKVSGH WLDETPGIYA
     TAVGVNGQRA MVLDLASTNP AGWAQDKGPT VKMPNEVVLW EAHVRDITSH ASSGSSRVGK
     FLGLTEKGTK SPKGFSTGID HMKELGVTHV HLLPSFDYRS IDESKLDQPQ FNWGYDPQNY
     NVPEGSYSSD PYNAEVRIKE FKQMVKEFHD NQLGVVLDVV YNHTGLTKGS NFNLEFPDYY
     YRQKEDGHYS DASACGNETA SERAMARKFI MESCKFWAKE YHIDGFRFDL MAIHDLETMN
     QLTAELKKIN PNIIIYGEGW TAGSSPLPDY AKALKANTHQ LTHTSAFSDD LRDAIKGSVF
     DEKSTGFVNG AKHTEESIKF GVVGSVPHPQ VEIHHVNYSK AFWAREPWQA VNYVSCHDNL
     TLFDKLKVSR PDASPEELKK MNLLSDAIVL TSQGTPFLHA GAELLRTKNG EHNSYNLPDA
     INQINWDWKA EHPDVFTYYK NLIALRKAHP AFWMPTTQMV NHHLEFVTTE PGLVGYKLKD
     YAHGDSWKNI LVYYNGREEA AEVPLHGEWT VAVEEEVIHL NGSRQVEGHI LVPPVSMLVL
     FQK
//