ID   U2YC62_STRCV            Unreviewed;       766 AA.
AC   U2YC62;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=ANG5_1030 {ECO:0000313|EMBL:GAD44502.1};
OS   Streptococcus constellatus subsp. pharyngis SK1060 = CCUG 46377.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus; Streptococcus anginosus group.
OX   NCBI_TaxID=1035184 {ECO:0000313|EMBL:GAD44502.1, ECO:0000313|Proteomes:UP000016985};
RN   [1] {ECO:0000313|EMBL:GAD44502.1, ECO:0000313|Proteomes:UP000016985}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG46377 {ECO:0000313|Proteomes:UP000016985};
RA   Maruyama F., Sakurai A., Ogura Y., Homma H., Takahashi N., Ohtsubo Y.,
RA   Hoshino T., Okahashi N., Nakagawa I., Kimura S., Fujiwara T., Hayashi T.,
RA   Shintani S.;
RT   "Genome Sequences of seven clinical isolates and type strains of anginosus
RT   group streptococci.";
RL   Submitted (SEP-2013) 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:GAD44502.1}.
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DR   EMBL; BASX01000007; GAD44502.1; -; Genomic_DNA.
DR   RefSeq; WP_022525633.1; NZ_BASX01000007.1.
DR   AlphaFoldDB; U2YC62; -.
DR   Proteomes; UP000016985; 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; 2.60.40.10; 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; 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   Pfam; PF03714; PUD; 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          303..660
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   766 AA;  88147 MW;  2CAD00AB5D0F8B4E CRC64;
     MLDYRVLIHY HNQLDNYAAY NMWKWQMNQW GEEASFFQRD DFGIQGNLSY KSNQALGYVH
     VIVKTIDWSH QSVDYSIQLL PPHLVTEIWI IEGDSQVYYS RQAAMTSPYY AKQDPHAFDM
     ALDSKRFDQH WGYQGWLGCR YDGKKAEFKL WAPTAKKVQL VVYKNGSNHS KIWKVYDLQR
     GKNFSKDHSE NTIGIWSRVI SDDLADRAYQ YQLEFEHHKT LTRDPYAEAT TEDGKRSVIL
     SPTERNPKHF QVKQGQQATW RLDNPCQAVI YEMHVRDLTK SSSSGVSKKY RGTFLGACQK
     GTKNRSGQAT GFDYIQSLGI NVVQLQPISD RHKEYDWHGN VTYNWGYDPQ NYNAPETSFS
     TNPTKPSQGM RDLKTMIQAY HDAGISVVID VVYNHIYSTY DSPFQATMPD YYYRMNPDGS
     FQNGTGVGSE TASEHEMFRK YMIDSLLYWV KEYNIDGFRF DLMGIHDIET MRQIREALDE
     IDPRILTYGE GWDMGIGLLP LDKAKKDNAF ELSNIGFFND TERDAIKGAE VYGGLKAGFV
     SGEATEAIIA KAILGSNELG TYLTPNQVVN YVEAHDNYNL HDLLVELHPD DDDLTRTKRI
     ELATAMNLLL QGMSFMELGQ EFSRSKLIAT GENGQTIQED HERAMNSYNA PDTVNQVNWD
     LIADHQESID YIKKIIHLKT MTKEFSYQHY EDIYQHVFVH SAHTGSGVVM FEVKDEKYYL
     IIFNASGQSY NIEDIGNLRL VAGNSRQVSD SFVEDLTATV FEVVEW
//