ID   A0A150APS1_9BACT        Unreviewed;       674 AA.
AC   A0A150APS1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
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=AVL50_03675 {ECO:0000313|EMBL:KXX71894.1};
OS   Flammeovirga sp. SJP92.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae;
OC   Flammeovirga.
OX   NCBI_TaxID=1775430 {ECO:0000313|EMBL:KXX71894.1, ECO:0000313|Proteomes:UP000075267};
RN   [1] {ECO:0000313|EMBL:KXX71894.1, ECO:0000313|Proteomes:UP000075267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SJP92 {ECO:0000313|EMBL:KXX71894.1,
RC   ECO:0000313|Proteomes:UP000075267};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-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:KXX71894.1}.
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DR   EMBL; LQAQ01000018; KXX71894.1; -; Genomic_DNA.
DR   RefSeq; WP_062615295.1; NZ_LQAQ01000018.1.
DR   AlphaFoldDB; A0A150APS1; -.
DR   STRING; 1775430.AVL50_03675; -.
DR   OrthoDB; 9761875at2; -.
DR   Proteomes; UP000075267; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; 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   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; IPR049117; pulA_all-beta.
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; PF21653; pulA_all-beta; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000075267};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..674
FT                   /note="pullulanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007558917"
FT   DOMAIN          198..574
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   674 AA;  75349 MW;  FBE03D6E2FCE914F CRC64;
     MKRLILLFSS IITTCMLFSS CDSTPADGHS GFDAKDFNSY PYYDGDLGIQ YSKNATTFKM
     WSPTASQVTV QLYEKGLGGK ASESIPMQAT EKGTWTLKVN KDLLGKYYTY QVQIGDQKLA
     ETPGIYATAV GVNGKRGQII DFNSTNPTGW ENDQRPELKE LTDAILYEIH VRDITIAENS
     GAKNKGKFLG LTETGTVSDK GLKTGIDHIE ELGITHVHLL PSFDYHSVDE TKLEEGTYNW
     GYDPENYNVP EGSYSTNPYD AAVRIKEFKQ MVQALHQKGI RVILDVVYNH TFSGDDSNFS
     LEVPQYYYRQ NEKGGYSDAS ACGNETASER VMARKYIVES VLYWAKEYHL DGFRFDLMGI
     HDIETMNILA KRLKMEVDPS ILIYGEGWNA AASPLPAEEQ AIKANTPKMK GVAAFSDDIR
     DGLKGSVFYD DEIGFIQGNK ELNETIKFGI VASTKHPQID YSKINYSKAP WAPTPSQTVT
     YVSCHDNHTL FDKLSISQPD ASKEEIKKMH KLTSAVVLTS QGIPFIHSGA EMLRTKGGEH
     NSYNKPDAIN KINWDWKFEN KDIFDYYQGL IEIRKAHPAF RMTSTEMITQ NLKFIDFKDP
     LIVGYTISNN ANNDSAKTIA VIFNANKTAK DISKFLPSGK WKVLVDGNKA SSKGIKTMSS
     VKIEGISALV LIQE
//