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Database: UniProt
Entry: Q8DT51_STRMU
LinkDB: Q8DT51_STRMU
Original site: Q8DT51_STRMU 
ID   Q8DT51_STRMU            Unreviewed;       743 AA.
AC   Q8DT51;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 111.
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:AAN59190.1};
GN   OrderedLocusNames=SMU_1541 {ECO:0000313|EMBL:AAN59190.1};
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007 {ECO:0000313|EMBL:AAN59190.1, ECO:0000313|Proteomes:UP000002512};
RN   [1] {ECO:0000313|EMBL:AAN59190.1, ECO:0000313|Proteomes:UP000002512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159 {ECO:0000313|Proteomes:UP000002512};
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H., Lin S., Qian Y., Li S., Zhu H.,
RA   Najar F., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN59190.1; -; Genomic_DNA.
DR   RefSeq; NP_721884.1; NC_004350.2.
DR   AlphaFoldDB; Q8DT51; -.
DR   STRING; 210007.SMU_1541; -.
DR   KEGG; smu:SMU_1541; -.
DR   PATRIC; fig|210007.7.peg.1372; -.
DR   eggNOG; COG1523; Bacteria.
DR   HOGENOM; CLU_004744_4_1_9; -.
DR   OMA; KMMRKFM; -.
DR   OrthoDB; 9761875at2; -.
DR   PhylomeDB; Q8DT51; -.
DR   Proteomes; UP000002512; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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; IPR013784; Carb-bd-like_fold.
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.
DR   SUPFAM; SSF49452; Starch-binding domain-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002512}.
FT   DOMAIN          245..616
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   743 AA;  85324 MW;  7E44E8C83C1F3F4D CRC64;
     MGRDASFSRF DNFGIVGNLV YESDTFQSQV YLIVKNADWS VRTPDFSINC NPGLSKSEVW
     IVQGDDTLYY SWQAAVASHA YNQRQPHAFD MAVNSKRFDY EWGFQGWLGF SYQEDKTEFR
     LWAPTARRVE LIIYSSTGEK SSVLKVLKMK RGENRTPDDH TKNTHGVWKR TVEGDLNYHA
     YRYRVYYRRR IFRDTRDPYS IAVTADGKRS VVIADTDLIP EGFKVKHRQE ASWRLSNPNQ
     AVIAEMHIRD FSKSETSGVR HENRGKFLGA FETGTKNLYG DQTSFDYLKS LGINYVQLQP
     VFDHHQTFNE DGSYAYNWGY DPENYNVPEA SFASNPHAPT ARILELKQLV QAYHDAGIGV
     IMDVVYNHTY SSTDSAFQLA VPDYYYRMNH DGSLQNGSGC GNETASEKEM FRKYMIDSIL
     YWIQAYNIDG FRFDLMGLHD VETMNAIRQA VDAIDPNILL YGEGWDMGIG LMPEDKAKKD
     NAYQMPRIGF FNDDVRNAIK GAEVYGDFKR GFVSGEPTEN KIAKGMLGSD ELSSYLVPNQ
     VLNYVEAHDN YNLNDLLMEL HPEDDKTTHI KRVELANSLG ILMQGMAFIE LGQEFLRTKL
     FPTGPDGELT HADKERAMNS YNAPDEVNQI DWNNVTLYKS TVNFVKELIR LKTQEEAFSY
     QTYEDIRKHV YVESAEYGSG LVIVSISSHD KIFKLIFNVS EKNAKIDMTQ DEKYDIILTN
     IKRFHKLSGQ LENLTATVFE LKK
//
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