ID Q0SSR7_CLOPS Unreviewed; 655 AA.
AC Q0SSR7;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 92.
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:ABG86867.1};
GN OrderedLocusNames=CPR_1522 {ECO:0000313|EMBL:ABG86867.1};
OS Clostridium perfringens (strain SM101 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=289380 {ECO:0000313|EMBL:ABG86867.1, ECO:0000313|Proteomes:UP000001824};
RN [1] {ECO:0000313|EMBL:ABG86867.1, ECO:0000313|Proteomes:UP000001824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM101 / Type A {ECO:0000313|Proteomes:UP000001824};
RX PubMed=16825665; DOI=10.1101/gr.5238106;
RA Myers G.S., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., Deboy R.T.,
RA Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA Paulsen I.T.;
RT "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT Clostridium perfringens.";
RL Genome Res. 16:1031-1040(2006).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000312; ABG86867.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0SSR7; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; cpr:CPR_1522; -.
DR Proteomes; UP000001824; Chromosome.
DR GO; GO:0051060; F:pullulanase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; 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; 2.60.40.1180; 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 InterPro; IPR007275; YTH_domain.
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.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR PROSITE; PS50882; YTH; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000313|EMBL:ABG86867.1};
KW Hydrolase {ECO:0000313|EMBL:ABG86867.1}.
FT DOMAIN 597..655
FT /note="YTH"
FT /evidence="ECO:0000259|PROSITE:PS50882"
SQ SEQUENCE 655 AA; 75982 MW; 0D76BB574D08AF76 CRC64;
MRRNFNSKEF NDKYYYDGEL GAIYNKEKTI FRVWSPEAKS LELLLYRDGN TESLIERDLL
HKKSNGLWEL VKKGDLNGVY YKYHIVGEDF EHDFVDPYCK ALGVNGYRAM VIDLKKTNPK
GWENEKKPSL ENPLDSILYE MHLRDFSIDE SSGVSLENRG KFLGIVEENT KVPGKEVKTT
LDHLKELGIT HVHLLPSFDF GTVDEERLDE EQYNWGYDPV NYNVPEGSYS KNPYKGEVRI
KEFKEMVLKL HKAGIRVVMD VVYNHTYSGE NSNLNLSYPG YYHRQDDFGN FSNGSGCGNE
LASERLMVRK YMVDSLKYWA REYHIDGFRF DLMALHDIET LKGIREELNK IDPSILIYGE
GWNGGESPLP KEEACFKCNI EKFDKLQIAA FSDDMRDGIK GHVSHLKDGG FVNGGEDFEE
SIKFGIVAST YHEGVDYNKV NYSDSPWANE PYQTVNYCSA HDNNTLHDKL KIVCENASEE
EIIEMNKLSA AIFLTSQGIP FIHSGEELLR TKINEKGEFI ENSYNSNDFV NKIDWTRKVK
YMDLFKYYKG LIELRKEYPL FRLESNKEIR EKISFIESKL GINEKGIVAY RLKDNNNEFI
VIFNSNNNEV KINLPKGLWG VMVNNKFSGK EIRDEARDFY DIIRKSAYVF KKISN
//
