ID W6T809_9LACO Unreviewed; 1339 AA.
AC W6T809;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
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 ORFNames=LFAB_06860 {ECO:0000313|EMBL:ETY74511.1};
OS Lactiplantibacillus fabifermentans T30PCM01.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=1400520 {ECO:0000313|EMBL:ETY74511.1, ECO:0000313|Proteomes:UP000019247};
RN [1] {ECO:0000313|EMBL:ETY74511.1, ECO:0000313|Proteomes:UP000019247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T30PCM01 {ECO:0000313|EMBL:ETY74511.1,
RC ECO:0000313|Proteomes:UP000019247};
RX PubMed=24558238;
RA Treu L., Vendramin V., Bovo B., Giacomini A., Corich V., Campanaro S.;
RT "Genome Sequence of Lactobacillus fabifermentans Strain T30PCM01, Isolated
RT from Fermenting Grape Marc.";
RL Genome Announc. 2:e00060-e00014(2014).
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:ETY74511.1}.
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DR EMBL; AWWK01000032; ETY74511.1; -; Genomic_DNA.
DR STRING; 1400520.LFAB_06860; -.
DR PATRIC; fig|1400520.3.peg.1341; -.
DR eggNOG; COG1523; Bacteria.
DR HOGENOM; CLU_004744_1_0_9; -.
DR OrthoDB; 9761875at2; -.
DR Proteomes; UP000019247; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR022263; KxYKxGKxW.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR011840; PulA_typeI.
DR NCBIfam; TIGR03715; KxYKxGKxW; 1.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
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; PF19258; KxYKxGKxW_sig; 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.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 3: Inferred from homology;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW Secreted {ECO:0000256|ARBA:ARBA00022512}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..43
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 44..1339
FT /note="pullulanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004883883"
FT TRANSMEM 1315..1333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1304..1339
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|PROSITE:PS50847"
FT REGION 69..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1131..1272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1339 AA; 142616 MW; 89E0D237DA648135 CRC64;
MQTKEVVQKN WRMWKHGKQW LFSASAMLGL AVGAGLSGMV ANADTTVTAA NTPTSSVVEN
VSVKPATAQP TMAPTVAPTT APTAAPTVAP TTAPTATPTT APTAAPTVAP TTAPTVTRTA
KIQATAVVAA VPTAKVTTTS TSVAPVKDST KVVIHYAGDG TKWVPYVWGA KPNGNGQQYS
WTGTDSYGNY ADIDLDQNYQ QVGILLKGAD SWDKDGAGEN RMATVDDSGK AEVWYQAGSD
DAQTVTPTFD NATVNVHYHS KVANGVTAYQ VWTDQTAKQT VNLDQTDVYG NQLGTVALTG
KAFSKVYVQP VGADATVREF TPLPDNQGTD IYLVADDDQA YYTPSFALAT ETVTSAAMNT
DHELTVTVGK KLTTAEAQQQ ITVGNNQVAS LTAVAPDSAG LSKTFTVTTT NPIDILQNNT
VAFDGNTKAV DIGNYVRSQA FDDKYYYAGD DSGATYTENR TQIKLWAPTA NKVTLRLYAS
TANDASATSV MTMTRGDKGV WTSVLDGNYQ GWAYDYALQF GNGTTTTTDD PYSKAVTVNG
NRSVIEDVNA VQPTDFNRMP TFSNPTDAVI YETSVRDFTK DANSGVTDKG KFLGMVESGT
QTASGQVTGL DYLKDLGVTH VQLMPMYDFS SIDETSSDPS YNWGYDPKNY DVPEGSYSTD
ATNPTTRIME MKEMINGFHK AGIRVIMDVV YNHVYSMDEQ AFQKVVPGYY FQYDADGHAT
NGTGVGNDIA SERKMVRKYI LDSVKYWATE YNLDGFRFDL MGILDVDTMN AIRAELNAID
PGILVYGEGW DMRATDKEIG AAQYNADKVD KNVGFFSDDI RNAIKGSEFG GINPGLVEGN
TKETTYDNDA QAFVAGFLGG QGYADATTSH PYQAPSQTIN YVACHDNRTL YDMLKALMPD
ESEANLIKRD KLATSMAILA QGVPFINAGQ EALRTKDGND NSYNSSDAIN DIDWNRVQAN
AELVNYFKSL LNLRKSENVF RLNDYDQIKQ TIKVLKSGEN GIFAFEYAAG GHKLYVLFNV
NDQAVNFDAV NLGLGRILLS SDTATKLGSM TSLAGLSTLV VREDLPQTVT INYCDAQGQI
VKTTTVTLIK FGDQVVLSAP TDYRMIGGES AVTYDDDSTA TTWTLNVPVE KVATSNPDDN
GNTTNPENGG STTNPDNNGT STNPDNGGST TNPDNNGNTT NSDNGGATTD PDSNGNTTNS
DNGGSTTNPD SNENNVTNLD NGGNTTDSTG KAVTTPVEST KVTPTPANGQ AAVSTKSVNG
HRAATTTGSI ANGDQVTTPA TAKTTVKAAT TVAPAKAAIG NHALPQTDET PAQSATLLGG
LLLMAAGVLG AVAPKRKRH
//