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Database: UniProt
Entry: Q21NA5_SACD2
LinkDB: Q21NA5_SACD2
Original site: Q21NA5_SACD2 
ID   Q21NA5_SACD2            Unreviewed;      1432 AA.
AC   Q21NA5;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   24-JAN-2024, entry version 98.
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=pul13A {ECO:0000313|EMBL:ABD79824.1};
GN   OrderedLocusNames=Sde_0560 {ECO:0000313|EMBL:ABD79824.1};
OS   Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Saccharophagus.
OX   NCBI_TaxID=203122 {ECO:0000313|EMBL:ABD79824.1, ECO:0000313|Proteomes:UP000001947};
RN   [1] {ECO:0000313|EMBL:ABD79824.1, ECO:0000313|Proteomes:UP000001947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-40 / ATCC 43961 / DSM 17024
RC   {ECO:0000313|Proteomes:UP000001947};
RX   PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA   Weiner R.M., Taylor L.E.II., Henrissat B., Hauser L., Land M.,
RA   Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA   Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA   Richardson P.M., Borovok I., Hutcheson S.;
RT   "Complete genome sequence of the complex carbohydrate-degrading marine
RT   bacterium, Saccharophagus degradans strain 2-40 T.";
RL   PLoS Genet. 4:E1000087-E1000087(2008).
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; CP000282; ABD79824.1; -; Genomic_DNA.
DR   RefSeq; WP_011467045.1; NC_007912.1.
DR   STRING; 203122.Sde_0560; -.
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; sde:Sde_0560; -.
DR   eggNOG; COG1523; Bacteria.
DR   HOGENOM; CLU_004744_5_0_6; -.
DR   OMA; DKIVPWY; -.
DR   OrthoDB; 3236218at2; -.
DR   Proteomes; UP000001947; 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; 3.
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; 4.
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; PF00128; Alpha-amylase; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000001947};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1432
FT                   /note="pullulanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004199797"
FT   DOMAIN          92..183
FT                   /note="Pullulanase carbohydrate-binding module 41"
FT                   /evidence="ECO:0000259|Pfam:PF03714"
FT   DOMAIN          219..329
FT                   /note="Pullulanase N2"
FT                   /evidence="ECO:0000259|Pfam:PF17967"
FT   DOMAIN          344..428
FT                   /note="Glycoside hydrolase family 13 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02922"
FT   DOMAIN          618..665
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00128"
FT   DOMAIN          913..1076
FT                   /note="Alpha-1,6-glucosidases pullulanase-type C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11852"
SQ   SEQUENCE   1432 AA;  154263 MW;  D4F988102EA34E4B CRC64;
     MNAIRNMLKV STLILLAVGL YACGGGSTVE SGKELLTCSV PQVPNSAGTE CVDPEPIQCA
     IPTVPDEKNE TCIVGANPDA PDPIVFPGPN QAILFFNKAD GDYEGYRLHN WNSETCNAYA
     EGSLAASWSN GLVHSGVDPV YGAYWLLDLV EGHDDCGHFI IHVGTDDAGK EMGGGDWIMP
     LAQDDPKFTR MNFTFSGVGS VFEFPVPSLG PQKVAIAGAA AHWLDIDTLV WNLDTTDVAD
     VKLHYSATAG ITVDDDSNVS GSTADLTFAT LSEELQQLVP HMASWPAFGN MLTASDVKPI
     VKGQLIAVAY NADGKAIAAT KVQRARVLDA LYTAGENDAD EATLGVVYDG ANINVSVWAP
     TATSVTLRVF DAAKTEVSSH TMNEDTSTGI WSFAGDSNLD RVFYQFELSV FHPLTQAIET
     VTTSDPYSVS LSTNGEYSQF VNLADDDLLP ENWNGHTVPT IANFEDAVIL EAHIRDFSIR
     DETVSEANRG KYLAFTETES NAVKYLQRMA ESGVTHFHML PANDIATVNE DESEQINLTS
     TVAELCAVKA DAPVCGEESD SATLISVLES YQYEPLAAQA LVESMRSLDG FNWGYDPHHF
     NAPEGSYASD PDGVARIKEM REMNKALHDL GLRVVLDVVY NHTSASGLWD NSVFDKVVPG
     YYHRYDENSG GIITSTCCDN TAPENRMMHK FVVDSLVLWA EAYKFDGFRF DIMGHIPKST
     ILEAREAVLA VDPNTYFYGE GWNWGEVENN RLFVQATQAN MAGTEVGTFN DRPRDDIRSA
     ALFNEDGSLD AQDHIRLGLA GTQADFILES NRGNMGTGST YARASYGLDP ADIINYVSKH
     DNETLWDQLQ YGLPESMSLE DRVRAHNIAA TIPVMSQGIP FFQLGVDMLR SKSMDRNGYD
     AGDWFNFVDY TMASNNWDVG LPLAQDNEVR WEEIDAISGR ISAPGMFELD YSSQVFSEFL
     QIRKSSPLFR LTTSADIIDR VGFHNIGNRQ QQGLIVMSID DGTGLADLDP ANDAIVVVIN
     GTNESQSHTV ATAAGFQLHS IQQSSVDSVV AGSTFTAGEG EGTFTVPALT TAVFVKPQGE
     AQGAGLSADV TQGAPDVVPF GDTVVYIRGD MNTWSTDNPL TYAGNGVYST TIALTGGTTY
     GFKFADAEWG ALGVNFGGAE GGDGVVTEGV DKNLFATNTN LSFTPAVDAT YVITFDASDS
     AAPVANIVNE EPYPGSTILL RGDMNSWGET DAFTYEGGRI YTFETTLDAG TYGFKVATGD
     WNTVNFGAAA EDENVVSLGE NVYLGSTNFN LSLTLAESTE LVFIFDMTNL DEPKLRVMNK
     AFFGDTAVYI RGDMNSWGAT DEVAYVGDGA YATTLTLAVG SYSFKVADAD WADVNFGPTS
     AEAAPIVLGA TNATLFNSPN NFSLTVETAG DFTFTVTGPD ATNPSLTVTA AN
//
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