ID A8F6N6_PSELT Unreviewed; 842 AA.
AC A8F6N6;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
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};
DE Flags: Precursor;
GN OrderedLocusNames=Tlet_1262 {ECO:0000313|EMBL:ABV33820.1};
OS Pseudothermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / NBRC 107922 /
OS TMO) (Thermotoga lettingae).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Pseudothermotoga.
OX NCBI_TaxID=416591 {ECO:0000313|EMBL:ABV33820.1, ECO:0000313|Proteomes:UP000002016};
RN [1] {ECO:0000313|EMBL:ABV33820.1, ECO:0000313|Proteomes:UP000002016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO
RC {ECO:0000313|Proteomes:UP000002016};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Foster B., Bruce D., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA Richardson P.;
RT "Complete sequence of Thermotoga lettingae TMO.";
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABV33820.1, ECO:0000313|Proteomes:UP000002016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO
RC {ECO:0000313|Proteomes:UP000002016};
RX PubMed=19307556; DOI=10.1073/pnas.0901260106;
RA Zhaxybayeva O., Swithers K.S., Lapierre P., Fournier G.P., Bickhart D.M.,
RA DeBoy R.T., Nelson K.E., Nesbo C.L., Doolittle W.F., Gogarten J.P.,
RA Noll K.M.;
RT "On the chimeric nature, thermophilic origin, and phylogenetic placement of
RT the Thermotogales.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5865-5870(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; CP000812; ABV33820.1; -; Genomic_DNA.
DR RefSeq; WP_012003296.1; NZ_BSDV01000001.1.
DR AlphaFoldDB; A8F6N6; -.
DR STRING; 416591.Tlet_1262; -.
DR CAZy; CBM41; Carbohydrate-Binding Module Family 41.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; tle:Tlet_1262; -.
DR eggNOG; COG1523; Bacteria.
DR HOGENOM; CLU_004744_1_0_0; -.
DR OrthoDB; 9761875at2; -.
DR Proteomes; UP000002016; 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; 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:UP000002016}.
FT DOMAIN 363..744
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 842 AA; 97334 MW; 39141CCF67C9B887 CRC64;
MKKSLFFIIV ILSAVIFAST TVIVHYHRFD GNYEGWNLWI WPVEPIFQEG RAYNFTEKDD
FGLKAVITLP MNSTKVGIII RLREWEEKDV AKDRFINIKD NEEEVWILQN VEEIYTSKPD
TSPRVFFAKL VDFSTIEVYT TDAIDLNTYL DKIVVGIDEQ TVSISSLEKV DPTDITRTNY
FRIKLSQPLK EEDLSRDIFL QIDGFKKSRV YAVEVLDELY YDGPLGTFYT PQYTEFYVWT
PVSKSVKLLL YQTSEQDQPA FVVDMQRNEK GVWYTRLDKD LDGWFYRYRY ESYGKIREGV
DPYAKALSLQ GKFGAIVDMR KADPEDWQQD SYVKLDSYVD AIIYEIHIAD MTGSWTSNVK
NKSSYLGLIE EGTIGPNGVT TGLEHIKELG VTHVHILPIY DFYTGDEVKR DFENQYNWGY
DPYHYMVPEG CYSSDPSNPK TRIYEVKKMV QTFHKNGIGV IMDVVFPHTY GVGEFSVFDQ
AVPYYYYRLG KMGQYLNESS CGNTTNSERL MMRRYILDTV VHWAKEYHVD GFRFDQMGLI
DRKTMAMVEK TLRQINPSVI IYGEPWGGWG VQPRFGKSQL LDLRIAVFND GIRDGIRGSV
FDPKAKGFVM GSVGKEIKIK RGVVGSINYD NKLIADFAYS PEQTINYVAC HDNHTLWDKN
VLAAKSDRRE WSEEELKSAQ KLAAAILLTS QGVPFFHAGQ DFCRTKQFNE NSYNAPISIN
ALDYERKAQF IDVFEYHKGL IKLRKSHPAF RLRTADDIRK HITFLESPKK VVAFLINEHV
NNDPWEGILV IFNGDIVEHE LILPDGEWNV VVDKERAGVD LLYKLSGTIE IPPISAMVMY
RE
//
