ID U2UTN2_STRPY Unreviewed; 1165 AA.
AC U2UTN2;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=HMPREF1231_1262 {ECO:0000313|EMBL:ERL21600.1};
OS Streptococcus pyogenes GA06023.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1115816 {ECO:0000313|EMBL:ERL21600.1, ECO:0000313|Proteomes:UP000016663};
RN [1] {ECO:0000313|EMBL:ERL21600.1, ECO:0000313|Proteomes:UP000016663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GA06023 {ECO:0000313|EMBL:ERL21600.1,
RC ECO:0000313|Proteomes:UP000016663};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
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:ERL21600.1}.
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DR EMBL; AWPJ01000104; ERL21600.1; -; Genomic_DNA.
DR AlphaFoldDB; U2UTN2; -.
DR PATRIC; fig|1115816.3.peg.510; -.
DR Proteomes; UP000016663; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.
DR CDD; cd02860; E_set_Pullulanase; 1.
DR Gene3D; 2.60.40.1110; -; 2.
DR Gene3D; 2.60.40.1220; -; 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; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR005323; CBM41_pullulanase.
DR InterPro; IPR014755; Cu-Rt/internalin_Ig-like.
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; IPR019931; LPXTG_anchor.
DR InterPro; IPR011838; Pullulan_Gpos.
DR InterPro; IPR040806; SpuA_C.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR NCBIfam; TIGR02102; pullulan_Gpos; 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; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF03714; PUD; 2.
DR Pfam; PF18033; SpuA_C; 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; 2.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1143..1160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1133..1165
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|PROSITE:PS50847"
FT REGION 57..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1165 AA; 128636 MW; B931336C1E21E649 CRC64;
MKKKVNQGSK RYQYLLKKWG IGFVIAATGT VVLGCTPSIL THQVAAKTIV GLARDEAQQG
DGNAKSGDGL QSSSKEAKPV LDSSSANPAS IAEHHLRMHF KTLPAGESLG SLGLWVWGDV
DQPSKDWPNG AITMTKAKKD DYGYYLDVPL AAKHRQQVSY LINNKAGENL SKDQHISLLT
PKMNEVWIDE NYHAHAYRPL KKGYLRINYH NQSGHYDNLA VWTFKDVKTP TTDWPNGLDL
SHKGPYGAYV DVPLKEGANE IGFLILDKSK TGDAIKVQPK DYLFKELDNH TQVFVKDTDP
KVYNNPYYID QVSLKGAEQT TPNEIKAIFT TLDGLDGDAV KQNIKITDKA GKTVAIDELT
LDKDKSVMTL KGDFKAQGAV YTVTFGEVSQ VARQSWQLKD KLYAYDGELG ATLAKDGSVD
LALWSPSADT VKVVVYDKQD QTKVVGQADL TKSDKGVWRA HLTSDSVKGI SDYTGYYYLY
EITRGQEKVM VLDPYAKSLA AWNDATATDD IKTAKAAFID PSKLGPTGLD FAKINNFKKR
EDAIIYEAHV RDFTSDKALE GKLTHPFGTF SAFVEQLDYL KDLGVTHVQL LPVLSYFYAN
ELDKSRSTAY TSSDNNYNWG YDPQHYFALS GMYSANPNDP ALRIAELKNL VNEIHKRGMG
VIFDVVYNHT ARTCLFEDLE PNYYHFMNAD GTARESFGGG RLGTTHAMSR RILVDSITYL
TREFKVDGFR FDMMGDHDAA AIEQAFKAAK AINPNTIMIG EGWRTYQGDE GKKEIAADQD
WMKATNTVGV FSDDIRNTLK SGFPNEGTAA FITGGAKNLE GLFKTTKAQP SNFEADAPGD
VVQYIAAHDN LTLHDVIAKS INKDPKVAEE EIHKRIRLGN TMILTAQGTA FIHSGQEYGR
TKQLLNPDYR TKVSDDKVPN KTTLIDAVAQ YPYFIHDSYD SSDAVNHFDW AKATDSIAHP
ISNQTKAYTQ GLIALRRSTD AFTKATKAEV DRDVTLITQA GQDGIQQEDL IMGYQTVASN
GDRYAVFVNA DNKTRKVVLP QAYRYLLGAQ VLADAEQAGV TAIAKPKGVQ FTKEGLTIDG
LTALVLKVSS KTADSSSQKS QTDNHQTKTP DGSKDLDKSL MTRPKRAKTN QKLPKTGEAS
SKGLLAAGVA LLLLAISLLM KRQKD
//
