ID C5CEA7_KOSOT Unreviewed; 693 AA.
AC C5CEA7;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
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=Kole_1455 {ECO:0000313|EMBL:ACR80147.1};
OS Kosmotoga olearia (strain ATCC BAA-1733 / DSM 21960 / TBF 19.5.1).
OC Bacteria; Thermotogota; Thermotogae; Kosmotogales; Kosmotogaceae;
OC Kosmotoga.
OX NCBI_TaxID=521045 {ECO:0000313|EMBL:ACR80147.1, ECO:0000313|Proteomes:UP000002382};
RN [1] {ECO:0000313|EMBL:ACR80147.1, ECO:0000313|Proteomes:UP000002382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1733 / DSM 21960 / TBF 19.5.1
RC {ECO:0000313|Proteomes:UP000002382};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Noll K.;
RT "Complete sequence of Thermotogales bacterium TBF 19.5.1.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACR80147.1, ECO:0000313|Proteomes:UP000002382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1733 / DSM 21960 / TBF 19.5.1
RC {ECO:0000313|Proteomes:UP000002382};
RX PubMed=21914881; DOI=10.1128/JB.05828-11;
RA Swithers K.S., Dipippo J.L., Bruce D.C., Detter C., Tapia R., Han S.,
RA Goodwin L.A., Han J., Woyke T., Pitluck S., Pennacchio L., Nolan M.,
RA Mikhailova N., Land M.L., Nesbo C.L., Gogarten J.P., Noll K.M.;
RT "Genome Sequence of Kosmotoga olearia Strain TBF 19.5.1, a Thermophilic
RT Bacterium with a Wide Growth Temperature Range, Isolated from the Troll B
RT Oil Platform in the North Sea.";
RL J. Bacteriol. 193:5566-5567(2011).
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; CP001634; ACR80147.1; -; Genomic_DNA.
DR RefSeq; WP_015868794.1; NC_012785.1.
DR AlphaFoldDB; C5CEA7; -.
DR STRING; 521045.Kole_1455; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; kol:Kole_1455; -.
DR eggNOG; COG1523; Bacteria.
DR HOGENOM; CLU_004744_4_1_0; -.
DR OrthoDB; 9761875at2; -.
DR Proteomes; UP000002382; Chromosome.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; 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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000002382}.
FT DOMAIN 214..597
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 693 AA; 78920 MW; 9E49DC61F2D85F44 CRC64;
MADFAVINSR REIRLFSSSI PSILLINGRR ASFIIDEFNG VKLIKVDFDL SVYDEVIIEL
SNGLSVPAYP VGLIDESEIT YDDWLGYKIE DDSIVLKVWA PGPQRLFIEI FESESSADLP
VVVPMELDKE TGVWSVKISK KFLNSAYRYR IERFGKILYS PDPYAPAATV NGKLSYILKF
DEFVPEGWES DEGPKLDSPV DAIIYEAHVK DLSTSWTANF QDRGKFVSLL EADASTVLGD
KAGIAHIREL GATHIQFLPL QDFGSVDEVD DNAYNWGYDP MLYNVPEGSY STDPCSPERR
ILEFRKLVSA VHKNGLGVIL DVVYNHTYVI DTPFNRLVPY YYYRLKENGE FSNGSGCGNE
LATERTMVRK FIIDSLKHWV RNYHVDGFRF DLMALLGKST VLEIERELRQ VKEDLLLYGE
PWSAASSSIK DVCLTKGEQR NINIAVFNDD LRNALKGYPD DESKGFVSGE RGWETGIVIG
MLGEIDYSHV FKGFTAHPTE TINYASAHDN LTLYDKLIKS VPKISFEERK RMAALALSII
LTSQGIAFIH AGSEMLRTKF LEENSYRSGS LINELNYLQK RIYRDFHEYI RGLILLRKNH
LLFRLRTADE VRRHVEVLHI ADGFVSVRLK DDQEEILVAH NARNEAVSLN ISGTWKLLVY
DCKIDLDGQR KVLDTIKVER LSTTVAIRMK DER
//
