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
//