ID A0A139NIH6_9STRE Unreviewed; 702 AA.
AC A0A139NIH6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=STRDD12_00957 {ECO:0000313|EMBL:KXT75845.1};
OS Streptococcus sp. DD12.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1777880 {ECO:0000313|EMBL:KXT75845.1, ECO:0000313|Proteomes:UP000070638};
RN [1] {ECO:0000313|EMBL:KXT75845.1, ECO:0000313|Proteomes:UP000070638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD12 {ECO:0000313|EMBL:KXT75845.1,
RC ECO:0000313|Proteomes:UP000070638};
RA Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I.,
RA Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.;
RT "Highly variable Streptococcus oralis are common among viridans
RT streptococci isolated from primates.";
RL Submitted (JAN-2016) 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:KXT75845.1}.
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DR EMBL; LQRG01000010; KXT75845.1; -; Genomic_DNA.
DR RefSeq; WP_066915640.1; NZ_KQ969495.1.
DR AlphaFoldDB; A0A139NIH6; -.
DR STRING; 1777880.STRDD12_00957; -.
DR PATRIC; fig|1777880.3.peg.982; -.
DR OrthoDB; 9761875at2; -.
DR Proteomes; UP000070638; Unassembled WGS sequence.
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; 2.60.40.2320; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 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; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR040697; PulA_N1.
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; PF17999; PulA_N1; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF81296; E set domains; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000313|EMBL:KXT75845.1};
KW Hydrolase {ECO:0000313|EMBL:KXT75845.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070638}.
FT DOMAIN 219..607
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 702 AA; 81799 MW; 99E0072512505F2D CRC64;
MTLRHFKAYL DDLQSLTICL PKRFPHQQIA FVLEEKDRHD QKIHTWIEQE YTDDDAIYYR
LSLQSPLDLE KRYLVYDSDR NVQALTYRHI VRTPIFDQTF DARNFRLGAS YQQTATIFRL
WAPISDEVWL QIEKDGHKES LALNYREKGV WELRLTGDWE GASYRYLHLV NGQWQEVHDP
YAISSTSNSG ASYVINPSRL HPVSPLKKEL PKAQAIVYEM SVRDFSAQDS AGFSHKRQFK
GLTESPKTGQ ASQGFDYLKE LGISHIQLMP LYDFGSVDEE HPRLCYNWGY DPVQYNVPDG
SFVSDPDHPY NRLTDLQDAI SLYHQAGIGV IMDVVYNHVY DIDQYAFEKI VPGYCYRVDL
AGKKSNGSWC GNDMATERLM MRDYIVKSVC YWAQTFDMDG FRFDLMGLID RQTISDIATQ
LKAIKPNAYL YGEGWEMGTG LDTQLLAHQN NAKYLPEIGF FNDSYRDTFK KVLTQPQRLL
DEHLHQKIEN LLSGSIGLSQ QTPAYLTADQ SINYLECHDN ATFFDYIRLK LPTIHRGWQE
HIASFGLQLQ LLSQGVCFIH SGQEFFRTKN HLENSYNSPD SINRLDWKRR QTYAENAQFI
SELIAFRKSE PLLALNQTEA IQKASHFYWL NPYVLRYNLY KDQRDLEIVI NFSTEHYVYP
NDDKRHLILQ YPDLNDQGVK ENIPLSPQSL IVLQKPTHPH EN
//
