ID A0A077MFF8_9MICO Unreviewed; 1938 AA.
AC A0A077MFF8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=BN13_50032 {ECO:0000313|EMBL:CCI53863.1};
OS Tetrasphaera jenkinsii Ben 74.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Tetrasphaera.
OX NCBI_TaxID=1193518 {ECO:0000313|EMBL:CCI53863.1, ECO:0000313|Proteomes:UP000035720};
RN [1] {ECO:0000313|EMBL:CCI53863.1, ECO:0000313|Proteomes:UP000035720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ben 74 {ECO:0000313|EMBL:CCI53863.1,
RC ECO:0000313|Proteomes:UP000035720};
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:CCI53863.1}.
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DR EMBL; CAJC01000161; CCI53863.1; -; Genomic_DNA.
DR RefSeq; WP_048543917.1; NZ_HF571038.1.
DR STRING; 1193518.BN13_50032; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000035720; 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; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000035720};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1938
FT /note="pullulanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039221809"
FT DOMAIN 155..612
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1612..1634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1938 AA; 206610 MW; 1EEE512CDBDB311B CRC64;
MHFRRSTAVI AAFFLAVVGY LPSVATAQAA ARTATLVGSL QSELGCDRDW NPECTATDLT
QVGTSSTYEK TFTVPAGSWE LKVAINHSWD EGYGAAGGGN IPLVLEGPAQ LTVAYDDETH
KVGLTPVIAG GVSAADKKGP LDSLRAGLTK ERFYFLMADR FANGSAANDT GGLTGDRLAT
GLDKTDTGFY HGGDLRGVIG KLDYIKGLGT TAIWLTPSFK NRPVQGSGAN ASAGYHGYWI
TDFTQIDPHL GTNAEMKELI TKAHAKGMKV FFDIITNHTA DVIDYANGGD YHYVSKASSP
YRDASGTAFD DRDYAGGTTF PTLDPATSFP YQPVFRTPAD ASVKVPAWLN DRTLYHNRGD
STFAGESSEY GDFVGLDDLF TERPEVVKGM GEIYKTWVDL GIDGFRIDTV KHVNLKFWEQ
FAPAILGHAA AIGNPDFFMF GEIFDSNPKF VSQYTTTGKL PAALDFSFQE AAIDFAGGSA
TTRLRDMFAG DDYFTDGDSN IYESPTFLGN HDRGRAAWMI QSKGFAGTEL LNRVKLANSL
MYLTRGQPIV YYGDEQGLIG SGGDKDARED LFATKVAQYA EEANLTGPSG SRNRYSTTAP
LYVQLRKLAA LRQANPALAD GAQIHRYASN DPGIYAFSRI RQGQNLEYLV VANNATTAKT
ASFNVTARNA GFTPLLGGTE VRANASARVT VTVPALSVRV FKAKAKLPAR TSAPAVYLTS
PAPGGVVSGR AQISAAVTQS AFAQATFRVR PVGTTAWQTI GTDDAQPYSV YHDVSAMAPG
TMLEYRVVLK DSSGNFSAKS SYAVVGAPGA KMAKPGTSTR SDRRGPSAIA SVNAVGPVTQ
PDAVAVAGSL DSELGCTGEN DGDWQPYCDQ AQMTLDPSDQ IWKLTVTIPA GEYEYKAALN
KSWTENYGLG GALGGANVKV TTDGNPVTFF YDHSTHWITS DANGPIITAP GSMQSELGCP
GDWQPDCMNP WLQDPDGDGT YTWRSDQLPV GNYEFKVAHG LNWDENYGVG GAPGGANVPF
SVSKAGVVVT ITYVLATHQI TVTTSSSGPA PDLKAAKAFW VTPTLLAWPA DAIPDGANPA
LLKWRLHYAP NAGMSIDAED LPGSKSLPLR YDSAGLPASV TSSYPELRGY LALRLNSVAA
QQAPTILRGQ VAVALYDNVG ALLDATGVQT AHVLDSLYAA SATTRSYGAT FAGTGGPTYR
VWAPTAKKVT LLTWSASAPG DAPISTAKRT AMIRATDGSW SVKAGAKNAR YLYEVVVYAR
STGKIETVRV TDPYSVALTL NSTRSVAVNL KDPTFRPTLW TTTKQPGLAR FADTSIYELH
VRDFSISDTS VPAEQRGSYL AFAGNGKGMQ HLKALRGAGL NTIHLLPTFD IASIQEDPAK
QSTPQCDLSS MAPDSEQQQA CIDAIRGNDA FNWGYDPWHW MAPEGSYAST PTAADGGKRV
AEFRTMVGGL HRAGLRVVLD QVFNHTPTSG LADTSVLDKV VPDYYQRLNA TGAVETSTCC
QNIATEHLMA QKAMVDAVVM WARDYKIDGF RFDLMGHHSR ANLLAVRAAL NKLTVTNSGV
NGKKVYLYGE GWNFGEVAGN ALFYQATQGQ LGGTHIGTFS DRLRDAVRGG GPFDEDPRKQ
GFGSGEFTDP NGAPINDAAA TTLKHDTDLV QLGLAANLKS FTFRLNSTGE VARGDQVDYN
GSPAGYATNP DEVITYVDAH DNETLFDSLT FKLPVATSMA DRVRMNTLSL ATTVLAQTPS
FWHAGTDLLR SKSLDRNSYD SGDWFNRLDW TGADNGFGHG LPLQGDNGAK WSYMRPLLAN
TSLKPSAGDV AQASAMAQDL LRVRYSSRLF RLGSAAAINA KVSFPVSGTA DAQPGVIVMR
IDDTVGADLD PSLAGALIVF NASPTTISQK VPGLSGVSLS LSPVQAGGAD PVVKTATWTA
STGTAGVPGR TVAVFLQK
//
