ID E9FJT1_9STRE Unreviewed; 759 AA.
AC E9FJT1;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 41.
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:EFX59561.1};
GN ORFNames=HMPREF0851_00537 {ECO:0000313|EMBL:EFX59561.1};
OS Streptococcus sp. M334.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=563038 {ECO:0000313|EMBL:EFX59561.1, ECO:0000313|Proteomes:UP000003840};
RN [1] {ECO:0000313|EMBL:EFX59561.1, ECO:0000313|Proteomes:UP000003840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M334 {ECO:0000313|EMBL:EFX59561.1,
RC ECO:0000313|Proteomes:UP000003840};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R.,
RA Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Mehta T.,
RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D.,
RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., Yandava C.,
RA Sibley C.D., Field T.R., Grinwis M., Eshaghurshan C.S., Surette M.G.,
RA Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Streptococcus sp. M334.";
RL Submitted (MAR-2010) 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}.
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; GL732486; EFX59561.1; -; Genomic_DNA.
DR RefSeq; WP_000283056.1; NZ_GL732486.1.
DR AlphaFoldDB; E9FJT1; -.
DR eggNOG; COG1523; Bacteria.
DR HOGENOM; CLU_004744_4_1_9; -.
DR OrthoDB; 9761875at2; -.
DR Proteomes; UP000003840; Unassembled WGS sequence.
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; cd02860; E_set_Pullulanase; 1.
DR Gene3D; 2.60.40.1110; -; 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 Glycosidase {ECO:0000313|EMBL:EFX59561.1};
KW Hydrolase {ECO:0000313|EMBL:EFX59561.1}.
FT DOMAIN 296..660
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 759 AA; 86460 MW; AACC7F6770BF4279 CRC64;
MYNYPMRIHY HRKNGEYDTC SFVKSQDQRI DLLTYKEDYF GALFSFEHPS SHPLESLNFV
VHTGQTSKEY AIRFNHYPLL TEVWILEGDD RIYYSENPAI ASPFYKNQNP FAFDKAINSA
SFDHHWGYQG ELGCRVEDNQ AHFALWAPTA TEVQVVVYES ATNDAPVWKT FEMERGNSYS
YNHKDNTIGV WSLDVEEDLT GKAYQYQVQF PHHQTLTRDP YTIATSPDGK RSAILSHEEK
QVANFEVKHG SEATWRLANP CKAVICEMHI RDLTKSPTSG VDEHLRGTFL GAAQTGTVNQ
YGQSTAFDHI KKLGYNYVQL QPIADRHKEY DADGNVTYNW GYDPQNYNAP ETSLSTNSED
PAQVIRDLKT MVQAYHDAGI GVIMDVVYNH TFSVVDAPFQ TTVPDYYYRM NPDGTFQNGT
GVGNETASEH EMFRKYMIDS LLYWVQEYNI DGFRFDLMGI HDVKTMQMIR QSLDEIDPNI
ILYGEGWDMG TGLAPYDKAK KDNAYQMPNI GFFNDNQRDA VKGGEVYGAI KSGFVSGAAT
EPILAKAILG SRELGTYTHP NQVLNYVEAH DNYNLHDLLA TLHPDQSSEK IMRKVETATA
MNLLMQGMAF MEIGQEFGRT KLVATGENGE LTHDDRERAM NSYNAPDSVN QVNWDLINER
QDSIEFIRQM IRLKTETSAF SYPTYEEIYH HVFVHSANEH SGWIVYEIHG EEHLLVVFNA
KGQDFQFENA GNLELLVTNS HLADKDMVGG VSASVFKVL
//
