PULA_THEMA
ID PULA_THEMA Reviewed; 843 AA.
AC O33840;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 2.
DT 25-MAY-2022, entry version 153.
DE RecName: Full=Pullulanase;
DE EC=3.2.1.41;
DE AltName: Full=Alpha-dextrin endo-1,6-alpha-glucosidase;
DE AltName: Full=Pullulan 6-glucanohydrolase;
DE Flags: Precursor;
GN Name=pulA; OrderedLocusNames=TM_1845;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=9453151; DOI=10.1111/j.1574-6968.1998.tb12793.x;
RA Bibel M., Brettl C., Gosslar U., Kriegshaeuser G., Liebl W.;
RT "Isolation and analysis of genes for amylolytic enzymes of the
RT hyperthermophilic bacterium Thermotoga maritima.";
RL FEMS Microbiol. Lett. 158:9-15(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; AJ001087; CAA04522.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD36907.1; -; Genomic_DNA.
DR PIR; H72204; H72204.
DR RefSeq; NP_229641.1; NC_000853.1.
DR RefSeq; WP_004082389.1; NZ_CP011107.1.
DR PDB; 2J71; X-ray; 1.69 A; A=18-120.
DR PDB; 2J72; X-ray; 1.49 A; A/B=18-120.
DR PDB; 2J73; X-ray; 1.40 A; A/B=18-120.
DR PDBsum; 2J71; -.
DR PDBsum; 2J72; -.
DR PDBsum; 2J73; -.
DR AlphaFoldDB; O33840; -.
DR SMR; O33840; -.
DR STRING; 243274.THEMA_04980; -.
DR CAZy; CBM41; Carbohydrate-Binding Module Family 41.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; AAD36907; AAD36907; TM_1845.
DR KEGG; tma:TM1845; -.
DR eggNOG; COG1523; Bacteria.
DR InParanoid; O33840; -.
DR OMA; KMMRKFM; -.
DR OrthoDB; 99080at2; -.
DR EvolutionaryTrace; O33840; -.
DR Proteomes; UP000008183; 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; cd10315; CBM41_pullulanase; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 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; IPR011840; PulA_typeI.
DR InterPro; IPR045041; Pullulanase_PULA-like.
DR PANTHER; PTHR43631; PTHR43631; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02922; CBM_48; 1.
DR Pfam; PF03714; PUD; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF49452; SSF49452; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR TIGRFAMs; TIGR02104; pulA_typeI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosidase; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..843
FT /note="Pullulanase"
FT /id="PRO_0000001428"
FT ACT_SITE 535
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 564
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT SITE 652
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT STRAND 21..28
FT /evidence="ECO:0007829|PDB:2J73"
FT STRAND 37..47
FT /evidence="ECO:0007829|PDB:2J73"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:2J73"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:2J73"
FT STRAND 63..72
FT /evidence="ECO:0007829|PDB:2J73"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:2J73"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:2J73"
FT STRAND 88..98
FT /evidence="ECO:0007829|PDB:2J73"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:2J73"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:2J73"
SQ SEQUENCE 843 AA; 96262 MW; C42DDE233D54FE77 CRC64;
MKTKLWLLLV LLLSALIFSE TTIVVHYHRY DGKYDGWNLW IWPVEPVSQE GKAYQFTGED
DFGKVAVVKL PMDLTKVGII VRLNEWQAKD VAKDRFIEIK DGKAEVWILQ GVEEIFYEKP
DTSPRIFFAQ ARSNKVIEAF LTNPVDTKKK ELFKVTVDGK EIPVSRVEKA DPTDIDVTNY
VRIVLSESLK EEDLRKDVEL IIEGYKPARV IMMEILDDYY YDGELGAVYS PEKTIFRVWS
PVSKWVKVLL FKNGEDTEPY QVVNMEYKGN GVWEAVVEGD LDGVFYLYQL ENYGKIRTTV
DPYSKAVYAN SKKSAVVNLA RTNPEGWEND RGPKIEGYED AIIYEIHIAD ITGLENSGVK
NKGLYLGLTE ENTKGPGGVT TGLSHLVELG VTHVHILPFF DFYTGDELDK DFEKYYNWGY
DPYLFMVPEG RYSTDPKNPH TRIREVKEMV KALHKHGIGV IMDMVFPHTY GIGELSAFDQ
TVPYYFYRID KTGAYLNESG CGNVIASERP MMRKFIVDTV TYWVKEYHID GFRFDQMGLI
DKKTMLEVER ALHKIDPTII LYGEPWGGWG APIRFGKSDV AGTHVAAFND EFRDAIRGSV
FNPSVKGFVM GGYGKETKIK RGVVGSINYD GKLIKSFALD PEETINYAAC HDNHTLWDKN
YLAAKADKKK EWTEEELKNA QKLAGAILLT SQGVPFLHGG QDFCRTKNFN DNSYNAPISI
NGFDYERKLQ FIDVFNYHKG LIKLRKEHPA FRLKNAEEIK KHLEFLPGGR RIVAFMLKDH
AGGDPWKDIV VIYNGNLEKT TYKLPEGKWN VVVNSQKAGT EVIETVEGTI ELDPLSAYVL
YRE
