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Database: UniProt
Entry: A0A0N1ADT2_9PROT
LinkDB: A0A0N1ADT2_9PROT
Original site: A0A0N1ADT2_9PROT 
ID   A0A0N1ADT2_9PROT        Unreviewed;       943 AA.
AC   A0A0N1ADT2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=IP80_06560 {ECO:0000313|EMBL:KPF49772.1};
OS   beta proteobacterium AAP65.
OC   Bacteria; Pseudomonadota; Betaproteobacteria.
OX   NCBI_TaxID=1523424 {ECO:0000313|EMBL:KPF49772.1, ECO:0000313|Proteomes:UP000037849};
RN   [1] {ECO:0000313|EMBL:KPF49772.1, ECO:0000313|Proteomes:UP000037849}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP65 {ECO:0000313|EMBL:KPF49772.1,
RC   ECO:0000313|Proteomes:UP000037849};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL   Submitted (AUG-2015) 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   -!- 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:KPF49772.1}.
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DR   EMBL; LJHW01000006; KPF49772.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N1ADT2; -.
DR   STRING; 1523424.IP80_06560; -.
DR   PATRIC; fig|1523424.3.peg.3834; -.
DR   OrthoDB; 9800174at2; -.
DR   Proteomes; UP000037849; Unassembled WGS sequence.
DR   GO; GO:0051060; F:pullulanase activity; 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; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.60.40.1130; Rab geranylgeranyltransferase alpha-subunit, insert domain; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR004193; Glyco_hydro_13_N.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR011839; Pullul_strch.
DR   InterPro; IPR024561; Pullul_strch_C.
DR   InterPro; IPR040671; Pullulanase_N2.
DR   NCBIfam; TIGR02103; pullul_strch; 1.
DR   PANTHER; PTHR43002; GLYCOGEN DEBRANCHING ENZYME; 1.
DR   PANTHER; PTHR43002:SF11; PULLULANASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF02922; CBM_48; 1.
DR   Pfam; PF11852; Pullul_strch_C; 1.
DR   Pfam; PF17967; Pullulanase_N2; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF81296; E set domains; 2.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000037849};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..943
FT                   /note="pullulanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005865577"
FT   DOMAIN          414..789
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   943 AA;  101958 MW;  C806B9205A6010FF CRC64;
     MHPAHRLSAV FTLGVWACAA TAQAAAPTTA ACAAGFETVL QAAPAAAAPL PAQAVWLNRQ
     WLRWPGLNAA PAGGGYRLHF SATGQINARP GAPVAGADGA LTLDLRSAAL PAALHQRWRW
     VGQGATLAVR AADQHRLREL LRGQLVLTLE DAEGRVLQAT RAQTPGALDD LYARAEQLPD
     LGATITRTRV RGGGDADGWR TGFRLWAPTA QAVHLCLHPG ADAPASAVHT LQRDKATGAW
     GLQLPGDLSQ AQATHGGHYY TYLVDVALPG GGVVRNRVTD PYSLSLNANS QRSWIGRLDD
     PRWLPEGWAQ TKRPATVRHN TDLVIYELHL RDFSVRDTTV PAAHRGSYLA FTHPQSAGMQ
     HLRTLAAAGL TDVHLLPVFD LATVPEQGCT SPDEAHLAAL PPDSEEQQAL VAATTAQDCF
     NWGYDPLHFT APEGSYATEA NDGGARILEF RRMVMALHRA GLRVGMDMVY NHTSASGQTP
     KSVLDRIVPG YYHRLNAQGG VETSTCCDNT ATEHRMMAKL MIDSAVVWAR DHRIDSMRFD
     LMGHQPRAAM ERLQRAVNRA AGQTIHLLGE GWNFGEVKDG ARFVQAAQKS LNGSGIATFS
     DRGRDAARGG GCCDGPAEVL KHQGWLNGLH YAPNPQAQAA GAGTRAELLR SADLIRAGLA
     GTLQGYRLQT ADGSVKRLDQ IDYAGQGAGY ASQPGEVVNY VENHDNPTLW DINLLKLPPD
     TPREDRARVQ VLGGALTAFS QGVAYLHAGV ELLRSKNLDR NSYDSGDWFN RIDWTLQDNY
     FGGGLPPKRE GEGLWPAARP LLARAAEIKP TPAEMRYSRD AFLDLLRIRA SSTLFRLRTA
     EEVQRRLTMF NTGPDQVATV AVGHLNGRGL RGARFAEVLY AINVAPEAAE LRLPTLRGRP
     LVLHPVHRGP GAADPRPAAQ AQWDPATATL RVPPRTALVY VRE
//
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