ID Q2SQA9_HAHCH Unreviewed; 1192 AA.
AC Q2SQA9;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 104.
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 OrderedLocusNames=HCH_00252 {ECO:0000313|EMBL:ABC27165.1};
OS Hahella chejuensis (strain KCTC 2396).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae; Hahella.
OX NCBI_TaxID=349521 {ECO:0000313|EMBL:ABC27165.1, ECO:0000313|Proteomes:UP000000238};
RN [1] {ECO:0000313|EMBL:ABC27165.1, ECO:0000313|Proteomes:UP000000238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2396 {ECO:0000313|EMBL:ABC27165.1,
RC ECO:0000313|Proteomes:UP000000238};
RX PubMed=16352867; DOI=10.1093/nar/gki1016;
RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA Oh T.K., Kim J.F.;
RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT algicidal agent.";
RL Nucleic Acids Res. 33:7066-7073(2005).
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}.
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DR EMBL; CP000155; ABC27165.1; -; Genomic_DNA.
DR RefSeq; WP_011394242.1; NC_007645.1.
DR AlphaFoldDB; Q2SQA9; -.
DR STRING; 349521.HCH_00252; -.
DR CAZy; CBM41; Carbohydrate-Binding Module Family 41.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; hch:HCH_00252; -.
DR eggNOG; COG1523; Bacteria.
DR HOGENOM; CLU_004744_5_0_6; -.
DR OrthoDB; 3236218at2; -.
DR Proteomes; UP000000238; Chromosome.
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 CDD; cd02861; E_set_pullulanase_like; 1.
DR Gene3D; 2.60.40.1110; -; 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; 2.
DR Gene3D; 2.60.40.1130; Rab geranylgeranyltransferase alpha-subunit, insert domain; 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; 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; PF03714; PUD; 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; 3.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000313|EMBL:ABC27165.1};
KW Hydrolase {ECO:0000313|EMBL:ABC27165.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000238}.
FT DOMAIN 540..910
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1192 AA; 127327 MW; 6405525FEDB67048 CRC64;
MKRCFTWNCR QGVSVLLALT LLTLFGCSNG GGDKGDGTSD GDDGLYTPTA SQAVIYYKRE
DNNYDGWGLH LWSASGAAFS SSEYISGGET SWSNPLPATG VSSKYGAYYV IDFDSANWSS
FNLIMHKGDD KDLGGQDHTY SKATLGDDAF SFSGVGVLYP DPLTSPPVAL EGAKAHWLDA
DLIAYNGSGS VRLYHSANAS ITVNPATGEL SGGETIELTS SSLSDQVKAR FPHLASYSAW
TLPDSVDAKA LLKEQLVVAQ FSTGGELRDA TQVQTRGALD ALYAEAAADA QLGAVTAGAT
VYKLWAPTAQ SVKLKRYDAD KNLLSADVMT EDSASGVWTF ASDQNDNGRY YRYEVKVYHP
QTGGVETFDV TDPYSLSLSA NSEYSQVADL NDAALQPSGW SADADPSAYA VAAPEDIIIY
ETHIRDFSGS DNNGTAAYNG KFLAYTEPGR ESMTHLQALK DAGLTHLHLL PAFDIATVDE
RQGARADLDS TKAEFCALRS AAALCGDTSV TDSATLRSVL EACDPASGCA QALMNDLRAL
DSFNWGYDPY HYTAPEGGYA NEPEGTSRIL EFRRMVKALH DMGLNVVMDV VYNHTNDAGA
AEKSVLDKIV PGYYQRLNPE SGAVENSTCC SNTATEAAMF QKLMEDSLVV WARDYHIDSF
RFDLMGHHPK SGIESALAKV RAVRSNVYFY GEGWNFGEVQ NDARFVQATQ LNMSGSQIGT
FTDRLRDAVR GGGPFDSADS LRANQGFANG LYTLPNEFNS GSDTEKATLL GLTDNIRVGM
AGNLTDFVLV DASGATNVGA NLDYNGQPTA YAKDPADTIN YVSKHDNQTL WDNNQYKIAT
DVSAQDRVRM QLLALSIPLL SQGVPFLHMG SEILRSKSMQ RDSYDSGDWF NKVDFSYADN
NWNVGLPRED KDGANWPLIQ SIIANANAQT SAAQITDAAA IFRDFLRIRS GSKLFRLESA
ADIKARVDFH NVGSSQIPGL IAMSIDDGTG LTDLDPDHDA IVAIINATGA QQTITVPSAS
GFQLIDAQAS GADPVAAGAT SSGDSFTVPA LTSAVFVKPQ GASQGAGLPV NYDNKDPSAI
PPYGATTVYL RGDMNGWSTD TPLTFSSNGD YVATLTLAAG SYGLKIADAD WAAINLGGGL
TLTPGETAAL TADGDNLSLT LTEESQVTFR FNASDKDATT LTVTTTAVTD IN
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