ID F9LXZ2_STRMT Unreviewed; 761 AA.
AC F9LXZ2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 38.
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:EGU65383.1};
GN ORFNames=HMPREF9965_1244 {ECO:0000313|EMBL:EGU65383.1};
OS Streptococcus mitis bv. 2 str. SK95.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1000588 {ECO:0000313|EMBL:EGU65383.1, ECO:0000313|Proteomes:UP000003858};
RN [1] {ECO:0000313|EMBL:EGU65383.1, ECO:0000313|Proteomes:UP000003858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK95 {ECO:0000313|EMBL:EGU65383.1,
RC ECO:0000313|Proteomes:UP000003858};
RA Durkin A.S., Radune D., Hostetler J., Torralba M., Gillis M., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (MAY-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGU65383.1}.
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DR EMBL; AFUB01000042; EGU65383.1; -; Genomic_DNA.
DR RefSeq; WP_000283098.1; NZ_AFUB01000042.1.
DR AlphaFoldDB; F9LXZ2; -.
DR PATRIC; fig|1000588.3.peg.1257; -.
DR eggNOG; COG1523; Bacteria.
DR OrthoDB; 9761875at2; -.
DR Proteomes; UP000003858; 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; 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:EGU65383.1};
KW Hydrolase {ECO:0000313|EMBL:EGU65383.1}.
FT DOMAIN 267..660
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 761 AA; 86644 MW; 370A426590D64AB8 CRC64;
MYNYPVLLHF HRKNGDYTAC SFSTDRDENK SSLTSETTYF GLQFSFTVTS QEKVDSFTFK
AEIDGVLKEY LVRFNYYPLL TEAWILEGDE TVYYSENPAI ASPYYKDQNP FAFDKAIHSA
SFDHHWGYQG ELGYSLSDYQ TSFKLWAPTA TAVQVVVYEN TSNDAPIWKT FNLERGNSYS
YSHKYNTIGV WSLDLDENLA GKAYQYQIEF PHHQTLTRDP YTIATSPDGK RSVILSHQDR
QVEGFKVKHG TEAPWRLENP CKAVICEMHI RDFTKSPTSG VPEELRGTFL GAAQTGTVNQ
YGQATAFDYI KELGCNYVQL QPIFDRHKEY DENGNVTYNW GYDPQNYNAP ETSFSSNPDD
PGQVIRDLKT MIQAYHDAGI GVIMDVVYNH TFSTVDAPFQ TTVPDYFYRM NRDGTFQNGT
GVGNETASEH EMFRKYMIDS ILYWVKEYNI DGFRFDLMGI HDVKTMQAIR WALDEVDPRI
LTYGEGWDMG TGLAPYDKAK KDNAYQMPNI GFFNDNQRDA IKGGEVYGAI KSGFVSGAAT
EPIVAKAILG SRELGSYLSP NQVLNYVEAH DNYNLHDLLA TLHPDKSSDQ IMRKVETATA
MNLLMQGMAF IELGQEFGRT KLIPTGEHGE LTPADRERAM NSYNAPDSVN QVNWDLINER
QDSIEFIRQI IRLKTQISAF SYPTYEEIYR HVFVHTAAEN SGWIVYEIHG GAEHLLVVFN
AKGTSFYFEN AGKLEMFLTN SRSKQENVID DISVAVLKVL S
//
