ID A0A0Q9LMJ1_9MICO Unreviewed; 1936 AA.
AC A0A0Q9LMJ1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, 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=ASG70_05405 {ECO:0000313|EMBL:KRE54896.1};
OS Phycicoccus sp. Soil748.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Phycicoccus.
OX NCBI_TaxID=1736397 {ECO:0000313|EMBL:KRE54896.1, ECO:0000313|Proteomes:UP000051855};
RN [1] {ECO:0000313|Proteomes:UP000051855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil748 {ECO:0000313|Proteomes:UP000051855};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE54896.1, ECO:0000313|Proteomes:UP000051855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil748 {ECO:0000313|EMBL:KRE54896.1,
RC ECO:0000313|Proteomes:UP000051855};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KRE54896.1}.
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DR EMBL; LMSC01000007; KRE54896.1; -; Genomic_DNA.
DR RefSeq; WP_056883323.1; NZ_LMSC01000007.1.
DR STRING; 1736397.ASG70_05405; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000051855; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..1936
FT /note="pullulanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006377912"
FT DOMAIN 161..628
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 581..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1603..1636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1621..1635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1936 AA; 206274 MW; 86C9C66675D106B2 CRC64;
MARRPLVAAL SGAALVVSGL LVPLSALPAH AAQRTVTLVG SLQSELGCGK DWDETCTATD
LAQVAGTTTY AKAVTVPAGT YEYKVAIDHS WDESYGAGGT KGGANLPLVL KGPAKLEFTY
DDTSHQIGVR PVRLSGPATR ADQAYAGDSL RQPLTKERYY FVMADRFANG DKANDLGGLS
GDRLKTGYDP TDKGFYHGGD LKGIQGKLDY IKGLGTTAIW LTPSFKNKPV QGTPGSESAG
YHGYWITDFT QVDPHLGTNA DLKALIAAAH AKGMKVFFDI ITNHTADVIN YQEQQYTYRD
KTAFPYKDAD GTVFDDKQYA GKPGFPAMDP ATSFPYTPVF TNPGDATAKV PAWLNDPTNY
HNRGDSTFAG ESAEYGDFVG LDDLFTEKLN VQQGMEDIYK SWVDFGVDGF RIDTVKHVNM
EFWQSFSPAM LEQARKDGND DFFMFGEVYD ARPLYMSQYT TTGKLPATLD FGFQAQATSW
AQGKAGTDLR DLYADDDYYT DTDSNAYELP TFLGNHDMGR VGFLLQGKDP VGPALMARVE
LADSLMYLTR GQPITYYGDE QGFVGYGGDK DARQDMFATK VEDRTKPDGS VDKGYASQPV
LGGTAGSQDR YSTSAPLYQH IKGLAAVRAA NPALADGAQV HRYASNNAGI YAFSRIDQGK
RVEYVVAANN ATTTSSATFA TYGHNQTFTP VYGASGAVRS GKDGRVSVSV PAQSVSVWKA
TSPMDKPKSA PPVYLTSPGA GDVVGGRAEI GAAIPANTFA QVSFLYRPVG TTGWKRLGTD
DNAPYRVFHD VTGFAKGTLL EYRAVAKDSA GHLSASSSYG IVGGPKASGG GDGGGVGPVT
QPDSVSVPGD HNSEMGCGGD WDPACPQAQL TLDPKDQVWK GSYTLPVAPH AYKAAIDKKW
DENYGAGGRS NGDNISYTVP ASGQVSFYYD HSTHWVTSDA EGDIITAPGS FQSELGCPAD
WSPDCMKPWL QDPDGDGTYT WSSDQLPAGT YEFKVAHGLT WDENYGAGGA PGGANISVTV
PADGMVTSIS YDLATHETTT KVARAGSAPD LTKQRAIWVN RDTVAWPAAM VPDGANPALL
KWRLAWSRTG GLTVDAEDIT GGSSAALRYD TKGLPAGVVA AHPELKGYLA LRLDRATAAQ
VPDILEGQVA VGMYDSLNRL LDATGVQTAY VLDDVYAAAA AKRAYGVSFA GTKPSYRLWA
PTAQKVNVLT WEPGSAADAP TSAATRTAMK RADDGSWSAT AGTRNSRYLY EVTVWVPTTG
KVETTQVTDP YSVALTLNST RSVAVDLGEA AYRPSLWSTT KAPALKQDVD STIYELHVRD
FSVGDPTVSG ENRGSYLAFA ENGNGTKHLK ALAAAGLNTV HLLPTFDIAS IEEDPAKQVK
PACDLKTYAP DSEQQQACIE PTRSGDAFNW GYDPWHWMAP EGSYASTPAK ADGGARVAEF
RTMVGALHQD GLRVVLDQVF NHTPTSGQAS TSVLDKVVPG YYQRLNASGA VETSTCCQNV
ATEHAMAQKA MVDAVVLWAK QYKVDGFRFD LMGHHSKANM LAVRSALDAL TLAKDGVDGK
RVYLYGEGWN FGEVANNARF EQATQGQLGG TGIGTFSDRL RDAVRGGGPF DDDPRTQGFG
SGEATDPNGD SAANPSAATR LKHDTDLVQL GMAGNLRTFS MRLNENGQVA QGKDVDYNGA
PAGYADQPDE VISYVDAHDN ETLFDSLAFK LPQATSMADR VRMNSISLAT TALAQTPSFW
HAGADLLRSK SLDRNSYDSG DWFNTLDWTG ADNGFGHGLP LKGDNEAKWP YMKPLLADSA
FKPSANEVQS ATAQAQELLR LRFSTPLFRL GSASAINAKV SYPASGTADS HAGVIAMRID
DTVGTDADPA LKGLVVVINA SPDAVTQKVP GLAGSSLSLS PVQASGADTV VKASTWDAAS
GSATVPARTV AVFVQH
//
