ID Q81PS2_BACAN Unreviewed; 852 AA.
AC Q81PS2; A0A2P0HEY1; E9RC20; E9RC21; Q6HXY6; Q6KS07;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 162.
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 OrderedLocusNames=GBAA_2728 {ECO:0000313|EMBL:AAT31844.1};
OS Bacillus anthracis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392 {ECO:0000313|EMBL:AAT31844.1, ECO:0000313|Proteomes:UP000000594};
RN [1] {ECO:0000313|EMBL:AAT31844.1, ECO:0000313|Proteomes:UP000000594}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor {ECO:0000313|Proteomes:UP000000594};
RX PubMed=18952800; DOI=10.1128/JB.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
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}.
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DR EMBL; AE017334; AAT31844.1; -; Genomic_DNA.
DR RefSeq; WP_001167507.1; NZ_VLYO01000002.1.
DR AlphaFoldDB; Q81PS2; -.
DR CAZy; CBM41; Carbohydrate-Binding Module Family 41.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR DNASU; 1087991; -.
DR GeneID; 45022571; -.
DR KEGG; bar:GBAA_2728; -.
DR PATRIC; fig|1392.231.peg.1613; -.
DR HOGENOM; CLU_004744_4_1_9; -.
DR OMA; KMMRKFM; -.
DR Proteomes; UP000000594; Chromosome.
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; 1.
DR CDD; cd02860; E_set_Pullulanase; 1.
DR Gene3D; 2.60.40.1110; -; 1.
DR Gene3D; 2.60.40.2320; -; 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; 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; PF03714; PUD; 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.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000000594}.
FT DOMAIN 353..752
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 852 AA; 97293 MW; 75BE8ACC8E8DE266 CRC64;
MQITKRLINK TVLLLTLIVM LSSIFSFQSV KAVSNSKTTE VIIHYKEQSG NTKDWNLWIW
GENSSGKSYE FTGEDEFGKY AKINIDGDYN RLGFIIRTNE WEKDGGDRWI ENIKDGRAEV
WILSGDEKVY NSKPSSDLSI QKATIDSFHE ITVTTNVPFN IKEKKIEMEG IKIKSISPYD
INSGDITNKV KIITEQKIDL KQTYKVKIEN LADTNTEIGK VIRSEEFDYL FYYGGNDLGN
IYTPQHTKFR VWAPTASEAK LVTYKKWNDK IGTEINMQQG EKGTWKAELK GNQKGLYYTY
KVKIGDKWTE AVDPYARAAS VNGDKGAVVD LEETNPKKWN TNKKPKLKNP EDAIIYELHV
RDLSIQPESG IKQKGKYLGV TEKGTKGPEG VKTGLDHMKD LGVTHVQLLP IFDYASVNEE
KVNEPQYNWG YDPKNFNVPE GSYSTNPYEP TVRITELKQM IQTLHDNNLR VVMDVVYNHM
YNAAESNFHK LVPGYYYRYN EDGTFANGTG VGNDTASERT MMRKFMIDSV TYWAKEYNLD
GFRFDLMGIH DYETMNEIRK AVNQIDPSII LHGEGWDLNT PLAAELKANQ KNAEKMKGIA
HFNDNIRDGL KGSVFEEKEN GFVNGKENME DRIKKGITAG IDYDTNSSTY QDPEQVLTYV
EAHDNHTLWD KLELTNPGDS EEVRKQIHKL SSSILLTSQG IPFLHAGQEF MRTKYGDHNS
YKSPDSINQM DWLRRATFNN EVDYMKGLIE LRKKYPAFRM TSAEQIKTHV SFIDAPKNTV
TYTIEGNKHE YFTVAHNANR EAVEITLPSK GPWKVLVDGK QAGSKPLYVV HDNKIKVPAL
SSIVLKSEKP IK
//
