ID A0A2T0B5B8_9CLOT Unreviewed; 715 AA.
AC A0A2T0B5B8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-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:PRR79062.1};
GN ORFNames=CLLI_11030 {ECO:0000313|EMBL:PRR79062.1};
OS Clostridium liquoris.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1289519 {ECO:0000313|EMBL:PRR79062.1, ECO:0000313|Proteomes:UP000239706};
RN [1] {ECO:0000313|EMBL:PRR79062.1, ECO:0000313|Proteomes:UP000239706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100320 {ECO:0000313|EMBL:PRR79062.1,
RC ECO:0000313|Proteomes:UP000239706};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium liquoris DSM 100320.";
RL Submitted (MAR-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:PRR79062.1}.
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DR EMBL; PVXO01000032; PRR79062.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0B5B8; -.
DR SMR; A0A2T0B5B8; -.
DR OrthoDB; 9761875at2; -.
DR Proteomes; UP000239706; 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; 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; IPR049117; pulA_all-beta.
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; PF21653; pulA_all-beta; 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:PRR79062.1};
KW Hydrolase {ECO:0000313|EMBL:PRR79062.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000239706}.
FT DOMAIN 208..614
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 715 AA; 82725 MW; 654EEA770D9A9A33 CRC64;
MNIYDLVVTS FNKINFIVDD ILNFKIQNII IKNGDSILKI DGYEVIKNKF QLTLSSSINI
KEESFVIYEN LKIKASYYSL FSTKEFNNRY YCSSELGYNY TKDHTSFKIW CPIAVNLHVL
IYKESESFTG EKPEKINMKE HPNGLWYCDV LGNLDGYYYT YEVDIYNDIY EAVDPYTVAV
GINGFRGAII DLNKTNPYDW YNDSSPRPRY FTDAVIYEVN VRDISSHPDS GIKNKGKFTG
IIEENTYSSH NISTGLAHIQ ELGVTHIQLM PIFDFSHRSV DEKNPIDYNW GYDPKNYNVP
EGSYSTDAFN PYCRIYELKK TIMELHKKGF CVNMDVVYNH LWDGIDNNFQ KIFPGYYFRY
NKDGSMSNGS GCNNDTASEN LMMKKFIIDS IKFWVKEYHI DGFRFDLMGL HDIETMNSIR
KELDTIDPSI MLYGEGWNLK TNLRDDEKAC KENSSKMPNI GHFNDMIRDT IKGSIFIPKD
TGYATGKDHM ECLLKICITA SLKFTDGDNG IFSNPCETIN YVSCHDNHTL WDKINLSCEN
ESLEDKKYMH KLCNGIILTS QGIPFLHSGV EFCRTKSMIE NSFKSSDSIN CIDWHRKALF
LDVCKYYKDL INLRKEHAGF RMNKKEDIKN HLIFLNNVPK NIVAFILKDH ANGDPWKSIL
IIYNPNKNAG ILNIPYNSWN LIGTRDKISL SPLKIIEGDK IELEPISMTI LYSNE
//