ID F1YYB6_9STRE Unreviewed; 770 AA.
AC F1YYB6;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 50.
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:EGE54197.1};
GN ORFNames=SPB_0235 {ECO:0000313|EMBL:EGE54197.1};
OS Streptococcus parauberis NCFD 2020.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=873447 {ECO:0000313|EMBL:EGE54197.1, ECO:0000313|Proteomes:UP000003732};
RN [1] {ECO:0000313|EMBL:EGE54197.1, ECO:0000313|Proteomes:UP000003732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCFD 2020 {ECO:0000313|EMBL:EGE54197.1,
RC ECO:0000313|Proteomes:UP000003732};
RA Stanhope M.J., Durkin A.S., Hostetler J., Kim M., Radune D., Singh I.,
RA Town C.D.;
RL Submitted (FEB-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:EGE54197.1}.
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DR EMBL; AEUT02000001; EGE54197.1; -; Genomic_DNA.
DR RefSeq; WP_003104494.1; NZ_AEUT02000001.1.
DR AlphaFoldDB; F1YYB6; -.
DR eggNOG; COG1523; Bacteria.
DR HOGENOM; CLU_004744_4_1_9; -.
DR Proteomes; UP000003732; 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; cd10315; CBM41_pullulanase; 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; IPR005323; CBM41_pullulanase.
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 Pfam; PF03714; PUD; 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:EGE54197.1};
KW Hydrolase {ECO:0000313|EMBL:EGE54197.1}.
FT DOMAIN 274..681
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 770 AA; 88791 MW; 6130AC30753E70D4 CRC64;
MINNTVIVHY HSQAGKYFDL SLWQWQDGKL GNDAYFSKFD SFGAVAVLDY EAPYFLSHAY
VIVKDQFWKK KTVDYRIERE YGLEKSEVWI VSDDPTPYYS RQAAISSRNY RVRNAHAYDM
AVNSQRFDKK WGFSGWLGYR YLENQTSFRL WAPTAEKVDL IFFDSTDNTA SVHRVYHMAR
GKGKNPDNHI LNRHGIWEIT IYGNHNYQSY VYRVHYRKQT FVETRDPYSI ATTANGRRSV
VIDPTNLVPE GFSVKHNQEA TWRLDNPNQS VIYEMHVRDF SISETSGVSP ENRGKFRGLF
EKGTKNPQGD ATCFDYVTNL GVTHIQLQPI FNYHQNIDEE GNYAYNWGYD PENFNVPEAS
YASTAHGPAS SILELKEAIQ AYHDAGLNVV IDVVFNHTYS SRDSAFQLSV PDYYYRMAPN
GLFLNGSGCG NETASEKEMF RKYMIDSILY WVHEYNVDGF RFDLMGLHDV ETMNQIRQAV
DKVDPRIILY GEGWDMGTGL ADYQKAKKEN ANLMPRIGFF NDTQRNAIKG AEVYGAFVEG
FVSGAATEDV IAKAILGSDE LNPFLSPEQV INYVEAHDNY NLNDLFWALN ENDSIEIHTK
RVQLATAMNI LMQGITFMQL GQEFLRTKLH ATGPLNELTQ EDKHRAMNSY NASDSVNQVD
WNLVTYEKDT IDFVKKLIFM KTKSDMFSFS TFDEIRRHVY IESATKGSGF ISFTIKNSIN
YQFIFSIYGK RLREAKENDI IITNDKRFHN DNLIINNLTA MILDITEKPE
//
