ID Q6NI76_CORDI Unreviewed; 604 AA.
AC Q6NI76;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 108.
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=DIP0902 {ECO:0000313|EMBL:CAE49418.1};
OS Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS gravis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=257309 {ECO:0000313|EMBL:CAE49418.1, ECO:0000313|Proteomes:UP000002198};
RN [1] {ECO:0000313|EMBL:CAE49418.1, ECO:0000313|Proteomes:UP000002198}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis
RC {ECO:0000313|Proteomes:UP000002198};
RX PubMed=14602910; DOI=10.1093/nar/gkg874;
RA Cerdeno-Tarraga A.M., Efstratiou A., Dover L.G., Holden M.T.G., Pallen M.,
RA Bentley S.D., Besra G.S., Churcher C., James K.D., De Zoysa A.,
RA Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S.,
RA Jagels K., Moule S., Quail M.A., Rabbinowitsch E., Rutherford K.,
RA Thomson N.R., Unwin L., Whitehead S., Barrell B.G.Parkhill.J.;
RT "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT NCTC13129.";
RL Nucleic Acids Res. 31:6516-6523(2003).
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};
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DR EMBL; BX248356; CAE49418.1; -; Genomic_DNA.
DR RefSeq; WP_010934655.1; NC_002935.2.
DR AlphaFoldDB; Q6NI76; -.
DR STRING; 257309.DIP0902; -.
DR KEGG; cdi:DIP0902; -.
DR HOGENOM; CLU_004744_4_1_11; -.
DR Proteomes; UP000002198; 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; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR004193; Glyco_hydro_13_N.
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; PF00128; Alpha-amylase; 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 Hydrolase {ECO:0000313|EMBL:CAE49418.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002198}.
FT DOMAIN 145..515
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 604 AA; 67478 MW; C9CE5636C1BC0217 CRC64;
MTTTNSYTGQ LGAFLTPHGD TCFRVWSPDA ATADLLIENH TVSMHPIGDG VWEAKLDGDR
HGQRYSYRLS LRGETIESVD PYARAVTANG THGVVVTQST PVPRMPAFTA PTDAIIYEAH
VRDLSIAPNS GIHNKGRFLG LTERDTHTTA GNPSGLDYIL SLGVTHIQLL PIFDFGSVDE
TGDLSYNAQY NWGYDPMNYN APEGSYSSNP NDPFTRIDEL KHTIRTLHDA GLRVIMDVVY
NHVYDTTTSP LERTAPGHYF RMTDDGTFHD GTFCGNETAS ENPMMRKFII DSVTHWATEY
GLDGFRFDLM GIHDVDTMNA IRTALDAIDP SIIILGEGWN LGNHPPHILP ANQHNAAHMP
RIAHFNDSLR DTLKGSTFHS NSRGLLTGDH NPKHMWTLFN NIKGAQHLPG LNFTSANHTV
NYIEAHDNHT LYDRLHLLLP DAPHDELIRR CQLATTIQYL ACGITFIHAG QEFARTKNNT
ENSYNSPDHI NAIDYDRAAQ HPHSVQLLRD LNNFRKTHTE LFPTEYDDIN ELYEATLVSG
DFLTYSVGKQ TTVAINFSTQ PRSIPTEGYF AVLLDDHVFP TDKQIETNSW TVAPLSVSIL
QQVS
//
