ID   A0A367GCW1_9FIRM        Unreviewed;       640 AA.
AC   A0A367GCW1;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
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:RCH47952.1};
GN   ORFNames=C4885_13550 {ECO:0000313|EMBL:RCH47952.1};
OS   Subdoligranulum sp. APC924/74.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Subdoligranulum.
OX   NCBI_TaxID=2086273 {ECO:0000313|EMBL:RCH47952.1, ECO:0000313|Proteomes:UP000253465};
RN   [1] {ECO:0000313|EMBL:RCH47952.1, ECO:0000313|Proteomes:UP000253465}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APC924/74 {ECO:0000313|EMBL:RCH47952.1,
RC   ECO:0000313|Proteomes:UP000253465};
RA   Fitzgerald B.C., Shkoporov A.N., Ross P.R., Hill C.;
RT   "Complete genome sequencing of Faecalibacterium prausnitzii strains
RT   isolated from the human gut.";
RL   Submitted (FEB-2018) 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:RCH47952.1}.
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DR   EMBL; PSQF01000088; RCH47952.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367GCW1; -.
DR   OrthoDB; 9761875at2; -.
DR   Proteomes; UP000253465; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
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; 2.60.40.1180; Golgi alpha-mannosidase II; 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; IPR013780; Glyco_hydro_b.
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   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253465}.
FT   DOMAIN          174..545
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   640 AA;  70285 MW;  70321BAEBACD6ED2 CRC64;
     MNETQVSQLP VYAGNDLGAV WRSSATAFRL WAPTACSAAL HRFATGTDAE PEAADLGTLA
     MQRSEGGTWY LELAGDLAGQ YYQYELQFPD GTSTVTADPY AHAAGAGGTR SMVLNQAAAV
     PDGWQKDERP AIPAHARSVW EVHVADFTAD PASGVPQAYR GKFMGFTVDG TTLNGDGVHP
     TGLNYLKRLG VTHVQLQPIF DFATVDEVSG EDYNWGYDPL NYNLPEGSYA TDAFHGEVRV
     RECRAMIQAL HSAGLGVVMD VVYNHTYYSY SWLERTVPGY WNRRWENGSL TNGSGCGCDL
     ASERTMVRKY LVDSCVYWAK EYHIDGFRFD LMALHDVETM NAIRAALDAL PGGEDILMYG
     EPWQGGSTRM EHGAIPANKQ AAGLLDSRIG FFCDNTRDAI KGGVFNAGSA GYINGDMHCG
     YQVLHSIPAW RGGQADFMPQ APGQVVQYVS AHDNYTLWDK LKCVARRGDY AAPDADLLAQ
     NRMAAGIYLT CQGLPFMQGG EEFARTKHGD HNTYRGPLEL NRLDWTRAAQ LEELVQYYHG
     LLEIRKAYPE LSGMAGDAEP CILSLPGWLI GFVPERRGES LPGRLAVYYN PERTRQWAAL
     PAGSWRYLCD GTRAAAEPFG PACRNAIELA PVSVTILKVE
//