ID A0A2M9HNQ2_9BIFI Unreviewed; 688 AA.
AC A0A2M9HNQ2;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
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:PJM78409.1};
GN ORFNames=CUU80_09500 {ECO:0000313|EMBL:PJM78409.1};
OS Bifidobacterium scaligerum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=2052656 {ECO:0000313|EMBL:PJM78409.1, ECO:0000313|Proteomes:UP000228755};
RN [1] {ECO:0000313|EMBL:PJM78409.1, ECO:0000313|Proteomes:UP000228755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TRED {ECO:0000313|Proteomes:UP000228755};
RA Mattarelli P., Modesto M., Bonetti A., Puglisi E., Morelli L.;
RT "Draft genome sequences of strains TRE 1, TRE D, TRE H and TRI 7, isolated
RT from tamarins, belonging to four potential novel Bifidobacterium species.";
RL Submitted (NOV-2017) 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:PJM78409.1}.
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DR EMBL; PGLQ01000009; PJM78409.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9HNQ2; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000228755; Unassembled WGS sequence.
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; 2.60.40.10; 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; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000228755}.
FT DOMAIN 201..591
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 688 AA; 76072 MW; 8B6733E9C0732AF0 CRC64;
MAVADWTPAE PALPCPDYPV YTDGDLGATP DAKGTTFRVW APTASGVTLR LFATGSAGEE
IVTDHAGRLM DITTIDGPYA ADDDPCAAGL VATHELTPGA DGTWLVRCDG VGHGVYYDYI
VRFPDGTEHR TADPWARGAG VNGRRSMVVD LSRTDPKGWD EDRRPHIPSH DLVIWETHIG
DFSNDPHSGV PFEHRGTYLA FTYPNTSVDG DGEFPTCVAY LKRLGVTAVQ LMPFYDYGSI
DESLARDDPR HGFNWGYDPL NYNVPEGSYS TDPFDGEVRI RECKQMIQAL HKAGIKVIMD
VVYNHMFSTD NWFERMIPGY ALRRREDGSF ADGSACTNDV ATEHPMMRKY IVDSVTYWAR
EYHIDGFRFD LMGLIDVDTM NAVRSALDQL PGGASISMHG EPWAARETAL VKGTILADKR
GMPYLSPRIG MFCDSTRDAV RGHVFYQKVP GYLTGAAADY ADDIRHAEDG WRGTLSGTAA
VGQLIQYVSA HDDLTLWDKL CATMRPLPVE ADYAAEGERC EDLMHANRLA AGIVFTAAGV
PFLLSGEEFA RTKHGVSDSF RSPVELNQLD WRRAQRLSGL VDHYAALIRL RQGNPAYFGG
ARMIVPRDDE VVVFRVGDDC VAINPTGETR VQAAVQLEMP GPYDEVAKIA PDDWQCIYCS
EPDAAPAGVE DRQLPLPPYS FTVWRRSR
//