ID   C1CEA5_STRZJ            Unreviewed;       759 AA.
AC   C1CEA5;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 78.
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 {ECO:0000313|EMBL:ACO19474.1};
GN   OrderedLocusNames=SPJ_1056 {ECO:0000313|EMBL:ACO19474.1};
OS   Streptococcus pneumoniae (strain JJA).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=488222 {ECO:0000313|EMBL:ACO19474.1, ECO:0000313|Proteomes:UP000002206};
RN   [1] {ECO:0000313|Proteomes:UP000002206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JJA {ECO:0000313|Proteomes:UP000002206};
RX   PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA   Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA   Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA   Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA   Rappuoli R., Moxon E.R., Masignani V.;
RT   "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT   closely related species.";
RL   Genome Biol. 11:R107.1-R107.19(2010).
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}.
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DR   EMBL; CP000919; ACO19474.1; -; Genomic_DNA.
DR   RefSeq; WP_000283064.1; NC_012466.1.
DR   AlphaFoldDB; C1CEA5; -.
DR   CAZy; CBM41; Carbohydrate-Binding Module Family 41.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; sjj:SPJ_1056; -.
DR   HOGENOM; CLU_004744_4_1_9; -.
DR   Proteomes; UP000002206; Chromosome.
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; cd02860; E_set_Pullulanase; 1.
DR   Gene3D; 2.60.40.1110; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR004193; Glyco_hydro_13_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
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   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   Glycosidase {ECO:0000313|EMBL:ACO19474.1};
KW   Hydrolase {ECO:0000313|EMBL:ACO19474.1}.
FT   DOMAIN          296..660
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   759 AA;  86547 MW;  9CECEF2C8531585E CRC64;
     MYNYPMRIHY HRKNGEYDTC SFVKSQDQRI DLLTYKEDYF GALFSFEHPS SHVIESLNFV
     VHTGQTSKEY SIRFNHYPLL TEVWILEGDD RIYYSENPAI ASPFYKNQNP FAFDKAINSA
     SFDHHWGYQG ELGCRVEDNQ AHFSLWSPTA TEVQVVVYES AANDAPVWKT FEMKRGNSYS
     YNHKDNTIGV WSLDVEEDLV GKAYQYQVQF PHHQTLTRDP YTIATSPDGK RSAILSHVEK
     QVENFEVKHG SEATWRLENP CKAVICEMHI RDLTKSPTSG VDEHLRGTFL GAAQAGTVNQ
     YGQSTAFDYI KKLGYNYVQL QPIADRHKEY DEDGNVTYNW GYDPQNYNAP ETSFSTNPDD
     PAQVIRDLKV MVQAYHDAGI GVIMDVVYNH TFSVVDAPFQ TTVPDYYYRM NPDGTFQNGT
     GVGNETASEH EMFRKYMIDS LLYWVQEYNI DGFRFDLMGI HDVKTMQMIR QSLDEIDSNI
     ILYGEGWDMG TGLAPYDKAK KDNAYQMPNI GFFNDNQRDA VKGGEVYGAI KSGFVSGAAT
     EPILAKAILG SRELGSYTHP NQVLNYVEAH DNYNLHDLLA TLHPDQSSEQ IMRKVETATA
     MNLLMQGMAF MEIGQEFGRT KLVATGENGE LTHDDRERAM NSYNAPDSVN QVNWNLINER
     QDSIEFIRQV IRLKTKTGAF SYSSYDEIYH HVFVHSAIEH SGYLIYEVHG KEHLLVVVNA
     KSEPYQFENA GNLAMLVTNS RSKEDNVLND ISLAVLSVL
//