ID A0A077M0R3_9MICO Unreviewed; 1927 AA.
AC A0A077M0R3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=BN12_630014 {ECO:0000313|EMBL:CCH79903.1};
OS Tetrasphaera japonica T1-X7.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Tetrasphaera.
OX NCBI_TaxID=1194083 {ECO:0000313|EMBL:CCH79903.1, ECO:0000313|Proteomes:UP000035721};
RN [1] {ECO:0000313|EMBL:CCH79903.1, ECO:0000313|Proteomes:UP000035721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T1-X7 {ECO:0000313|EMBL:CCH79903.1,
RC ECO:0000313|Proteomes:UP000035721};
RX PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA Nielsen K.L., Nielsen P.H.;
RT "A metabolic model for members of the genus Tetrasphaera involved in
RT enhanced biological phosphorus removal.";
RL ISME J. 7:543-554(2013).
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:CCH79903.1}.
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DR EMBL; CAJB01000396; CCH79903.1; -; Genomic_DNA.
DR RefSeq; WP_048551870.1; NZ_HF570958.1.
DR STRING; 1194083.BN12_630014; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000035721; Unassembled WGS sequence.
DR GO; GO:0051060; F:pullulanase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11339; AmyAc_bac_CMD_like_2; 1.
DR CDD; cd11341; AmyAc_Pullulanase_LD-like; 1.
DR CDD; cd02860; E_set_Pullulanase; 1.
DR CDD; cd12962; X25_BaPul_like; 3.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR Gene3D; 2.60.40.1130; Rab geranylgeranyltransferase alpha-subunit, insert domain; 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; 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; PF11852; Pullul_strch_C; 1.
DR Pfam; PF17967; Pullulanase_N2; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF81296; E set domains; 2.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000035721};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..1927
FT /note="pullulanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001721054"
FT DOMAIN 162..618
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1599..1624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1927 AA; 205754 MW; B427EDFE621273BE CRC64;
MPLARRAYAV LAAAALGATT LVVGATPRAV AATDTVTIAG SLQSELGCSA DWDPSCTATD
LTRLGDTSIF ERTFTVPAGS YELKAAVNHS WDENYGAGGA SNGPNIPLVL QGPSTLLFSY
DDTTHQVGIS PTDLPGTTTT SADRKLATSS LRQPLTRERY YFVMADRFAN GDPSNDEGGL
TGGRLTTGYD PTDKGFYHGG DIKGITQRLD YIKGLGTTAI WLTPSFKNRP VQGTGDDASA
GYHGYWITDF TQIDPHLGTN ADLKTLIAKA HQKGMKVFFD IVTNHTADVI DYTQKEYTYR
NKTDYPYRDA SGNVFDDAQY AEKPDFPALD PATSFPYTPV FDSEADRTAK VPAWLNDPTN
YHNRGDSTYA GESATYGDFA GLDDLFTEKL SVEQGMEEIY KAWVDFGVDG FRIDTVKHVN
TEFWQRFSPA MLAEANRIGN KDFFMFGEVY DARPSFMSEY TTTAKLPATL DFGFQSQAVS
WVQGKSGTDL RDLYADDDYY TDTDSNAYEL PTFLGNHDMG RVAMMLKGTS TSDADLMAKV
GLADDLMFLT RGQPVTYYGD EQGFIGLGGD KDAREDMFAT KTQQYADEPV LGGPSGSMDR
YDTNAPLYQH IKQLSALRAA YPALADGAQV HRYASSGAGV FAFSRIDTAT NTEYVVALNN
ATTAKSATFA TYGRSQGFTP IYGAATRVRS AKDGRLTVTV PAQSVSVWKA AGRMVTPKNK
PALQQTSPSA GGVVGGRAEI SAAIPSGAFA QVSFAYRPVG TTTWKPLGTD DNAPYRVFQD
VSGMPKGTLL EYRTVAKDIA GHVSATSTYG IVGDPQTGGG GGGGVGPVTQ PDAVSVPGSH
NTEMGCPADW APDCDEAQLA LDPNDEIWKG TYTDLPAGPY AYKAAIDKSW DENYGAGAVK
NGANIEYTAG ASPVSFYYDH ATHWATSDAE GAVVTAPGSY QNELGCSADW DPACMRPWLE
DPDGDGTYSW TTDQVPAGSY EFKVAEGLSW DTSYGAGGVA GGSNIPLTVP ADGMLVTISY
VKATHAITAT VTRAGATPDL TKQRAIWVQR GLLAWPADMV PEGTDPRLLS WRLAWSRDGG
LAVDAEAVTG GSEARLTYDA KGLPKKVVTA HPELAGYLAL RLDRPAQRLV PDILQGQVAV
GEYDTLGRLQ DATSVQIAYV LDDLYAAKAA KTTLGVTFSG RVPTYRLWAP TAQSVDVLTW
PASAAADAPV ADATRTPMTR RPDGSWNAAV GSRGDRYLYD VVVYAPTART VEHNLVTDPY
SVALTLNSTR SVAVDLRDPA YQPAPWRTAP SPRLARGVDS TIYELHVRDF SIGDPTVPAA
HRGTYLAFAD DGDGTKHLKA LAQAGLNTVH LLPTFDIASI EEDRAKQETP ESAGCGDLSA
YAPDAEKQQA CIDSIRAKDG YNWGYDPFHV MAPEGSYASS AAAADGGARV AEFRTMVGAL
HRDGLRVVLD QVFNHTPASG EAPTSVLDQV VPGYYQRLDR TGVVYTSTCC QNVATEHAMA
QKWMVDTVVS WARNYKVDGF RFDLMGHASK ANLLAVRAAL DRLTLTKDGV DGRSIYLYGE
GWNFGEVADN ALFVQASQGQ LGGTGIGTFS DRLRDAVRGG GPFDDDPRKQ GFGSGEATDP
NGAAINDGAD ASLQHDTDLV QLGLAGNLRS FVFTDTEGAS VRGDEVDYNG SPAGYADQPD
EVISYVDAHD NETLWDSLTY KLPVATSMAD RVRMNTLSLA TTALAQTPSF WHAGADLLRS
KSLDRNSYDS GDWFNTLSWT GADNGFGHGL PLAGDNSSKW PFQQPLLANA ALKPSASDVG
AASAQAQDLL RLRFSTPLFR LGSASAIKQK VSFPASGTAA AHPGVIAMRI DDTKGRNADP
SLKGLVVVFN ATPSAVTQVV PGLAGKALSL SPVQANGSDP VVKGASWNAT TGAATVPART
VAVFVQR
//
