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
//