ID E8UBD1_DEIML Unreviewed; 1111 AA.
AC E8UBD1;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
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=Deima_2740 {ECO:0000313|EMBL:ADV68370.1};
OS Deinococcus maricopensis (strain DSM 21211 / LMG 22137 / NRRL B-23946 /
OS LB-34).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=709986 {ECO:0000313|EMBL:ADV68370.1, ECO:0000313|Proteomes:UP000008635};
RN [1] {ECO:0000313|EMBL:ADV68370.1, ECO:0000313|Proteomes:UP000008635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21211 / LMG 22137 / NRRL B-23946 / LB-34
RC {ECO:0000313|Proteomes:UP000008635};
RX PubMed=21677853; DOI=10.4056/sigs.1633949;
RA Pukall R., Zeytun A., Lucas S., Lapidus A., Hammon N., Deshpande S.,
RA Nolan M., Cheng J.F., Pitluck S., Liolios K., Pagani I., Mikhailova N.,
RA Ivanova N., Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brambilla E.M., Rohde M., Goker M., Detter J.C., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Deinococcus maricopensis type strain (LB-
RT 34).";
RL Stand. Genomic Sci. 4:163-172(2011).
RN [2] {ECO:0000313|Proteomes:UP000008635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21211 / LMG 22137 / NRRL B-23946 / LB-34
RC {ECO:0000313|Proteomes:UP000008635};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Kyrpides N.,
RA Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., Zeytun A.,
RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Pukall R., Gehrich-Schroeter G.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Deinococcus maricopensis DSM 21211.";
RL Submitted (JAN-2011) 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061}.
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DR EMBL; CP002454; ADV68370.1; -; Genomic_DNA.
DR RefSeq; WP_013557874.1; NC_014958.1.
DR AlphaFoldDB; E8UBD1; -.
DR STRING; 709986.Deima_2740; -.
DR KEGG; dmr:Deima_2740; -.
DR eggNOG; COG0366; Bacteria.
DR eggNOG; COG1523; Bacteria.
DR HOGENOM; CLU_004744_5_0_0; -.
DR OrthoDB; 9761875at2; -.
DR Proteomes; UP000008635; 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; 2.
DR CDD; cd02860; E_set_Pullulanase; 1.
DR Gene3D; 2.60.40.1110; -; 2.
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 Gene3D; 2.60.40.1130; Rab geranylgeranyltransferase alpha-subunit, insert domain; 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; IPR011839; Pullul_strch.
DR InterPro; IPR024561; Pullul_strch_C.
DR InterPro; IPR040671; Pullulanase_N2.
DR NCBIfam; TIGR02103; pullul_strch; 1.
DR PANTHER; PTHR43002; GLYCOGEN DEBRANCHING ENZYME; 1.
DR PANTHER; PTHR43002:SF11; PULLULANASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF02922; CBM_48; 1.
DR Pfam; PF03714; PUD; 2.
DR Pfam; PF11852; Pullul_strch_C; 1.
DR Pfam; PF17967; Pullulanase_N2; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF81296; E set domains; 2.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000008635};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1111
FT /note="pullulanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003232398"
FT DOMAIN 574..956
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1111 AA; 119724 MW; C72B9850419765B6 CRC64;
MKRFATLLTF ALTAQAVALT GPAFPAVPAL PALIAQAAAT LTPALPIAQN VLRVRYVRPD
GQYTGWGLHV WEDTTAAVEW AKPLAPTGID ANGAYWDVPL KAGAAKVGFI VHNGDEKDPG
ADLFADPGQG REVLVRSGVA DFTYVTSDAP VPDGVARLHY HRPDGQYDGW GLHAWEDTTA
TVEWSKPLPP TGTDAFGAYW DVPLKADWAK LSFIVHKGDE KDPGADMRLE RTAGNQGWIV
SGQDQVYTQK PDVTVRQIGD LTKQQAHWLT RDLIAVKPEL VADGAIVNLH YSLTGDLKLT
AAGVQGGQTL PLIPVPGGLS AALKAKYPHL AAYALVQVRP EEAAQVPGAL RGQLAVSSTR
LDDTLVDATG VQTYGALDDL DTYTGPLGAQ WQGNKPTLRL WAPTAQAVKL HVWLDGQERV
LPMVAGAQGV WSIAGDATWN GASYVYEVKV FAPSTGKVET NLVTDPYSLA LTRGSARSVL
VDLNDPALKP PGWDALRKPA LASASDLSFY ELHLRDFSVD DATVPAAQRG TYLAFTQAGS
AGMRHLRALA DAGLKAVHLL PTFDIATISE DKAAWKTPGD LSRLAPNSDA QQAAVNAVKE
QDAYNWGYDP YHYMVPEGSY AVNPDARTRE YRQMVMALNG AGLRVVQDVV FNHTNASGQA
ERSVLDRIVP GYYHRLDLNG AVTNSTCCSN TATEHNMMRR LMVDTLVLYA RQYKIDAFRF
DLMGHHMVED LRAVRAALDA LTVQKDGVDG RSVYVYGEGW DFGEVAQNAR GANATQRNLY
GLGIGTFNDR IRDAIRGGSP FGGLQDQGFA TGLVSLPNGQ PQNTDKARLL RLTDQIKVGL
SGNLRDFTFT DSAGKKVTGA GVDYNGQPTG YAASPREAIN YASAHDNQTL FDGVLLKAPV
NATTAQRVRM QNLAHSLVLL GQGLPFSQAG DDLLRSKSFD TDSYNSGDWF NMIDWTGRDN
GFGRGLPPAE KNAAQWDLYR PLLGNAALKP TQADAQRAAD HYREMLRVRY STPLFRLPTA
QAVQQALTFL NADPGVIVMK LSGSQGPYRN VVVVFNGTGT ATNVRDAALN GLKLDLHPAL
QKSSDALVRT SKASNGTLSV PALTTAVFVG K
//
