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Database: UniProt
Entry: A0A3P2ALP3_9FIRM
LinkDB: A0A3P2ALP3_9FIRM
Original site: A0A3P2ALP3_9FIRM 
ID   A0A3P2ALP3_9FIRM        Unreviewed;      2522 AA.
AC   A0A3P2ALP3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=pulA {ECO:0000313|EMBL:RRD96108.1};
GN   ORFNames=EII17_00955 {ECO:0000313|EMBL:RRD96108.1};
OS   Clostridiales bacterium COT073_COT-073.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales.
OX   NCBI_TaxID=2491044 {ECO:0000313|EMBL:RRD96108.1, ECO:0000313|Proteomes:UP000266937};
RN   [1] {ECO:0000313|EMBL:RRD96108.1, ECO:0000313|Proteomes:UP000266937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COT073_COT-073 {ECO:0000313|EMBL:RRD96108.1,
RC   ECO:0000313|Proteomes:UP000266937};
RA   Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA   Eisen J.A., Holcombe L.J., O'Flynn C.;
RT   "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT   for Automated Genome-Based Taxonomic Assignment.";
RL   Submitted (NOV-2018) 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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061}.
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:RRD96108.1}.
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DR   EMBL; RQYD01000002; RRD96108.1; -; Genomic_DNA.
DR   OrthoDB; 9761875at2; -.
DR   Proteomes; UP000266937; Unassembled WGS sequence.
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; cd02857; E_set_CDase_PDE_N; 1.
DR   CDD; cd02860; E_set_Pullulanase; 1.
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; 2.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR004185; Glyco_hydro_13_lg-like_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; IPR001119; SLH_dom.
DR   NCBIfam; TIGR02104; pulA_typeI; 1.
DR   PANTHER; PTHR43002; GLYCOGEN DEBRANCHING ENZYME; 1.
DR   PANTHER; PTHR43002:SF11; PULLULANASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF00128; Alpha-amylase; 2.
DR   Pfam; PF02922; CBM_48; 1.
DR   Pfam; PF00395; SLH; 3.
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.
DR   PROSITE; PS51272; SLH; 3.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000313|EMBL:RRD96108.1};
KW   Hydrolase {ECO:0000313|EMBL:RRD96108.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266937};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          2335..2395
FT                   /note="SLH"
FT                   /evidence="ECO:0000259|PROSITE:PS51272"
FT   DOMAIN          2396..2459
FT                   /note="SLH"
FT                   /evidence="ECO:0000259|PROSITE:PS51272"
FT   DOMAIN          2461..2522
FT                   /note="SLH"
FT                   /evidence="ECO:0000259|PROSITE:PS51272"
FT   REGION          266..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2086..2164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..283
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2094..2125
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2126..2154
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2522 AA;  285288 MW;  DF9C934702211AD0 CRC64;
     MNHKIKIQLS NPFIHLTFRR LLSWLLILTI FFSLPISTTS VYAENSGRYI QVQYNTDRDS
     FDFKIKADGA DYAYIRGDFT DNWAIQEEFK AVRRDEDNDK TGEMLLTVPA EKTENTGHQY
     KAYIYYADES QVPAEIRDGG NPHFGWMTAD GWNQNSNENL PARDFKANRS VMTEYQPSVA
     GAEDKVTFKI KANKAKHGYV MCDGNDWNVN TAEEKYKFTR TADDIREVEL MQVQIDYRDL
     IKGEHNQGYK VVLSYDGHSY EWMNAEGDSS GSAPNSSLPD RTGMPQIPNP GGQADRTVMT
     EYDQADDAVI FKLKADGYDY AYLMCQANNW TEADSYKMER DSSDTEKKEI LSLTLPYAQL
     ISREQMYQYK VKLYKSGQPD GEWINAEGNN GDNSLFPESP ITLPANVPFS PDQKSVQTIY
     HAGQSGQENK VEFRIKADGI DEAYVMCKAN QWATDNLADL ADYKAIRHKN DGNKNGLLTV
     TIPYSKLSST EQKYEYKIYA KSNGNAIWFN AEGLDANNSF FPTENNGEFG EIIHSAVMDE
     KDKIKVYLKP EYQNLDITYD IWVDDVKYPA IIESQDFLDI EVEYQNPWHL RRVTLDISQL
     WQRPDFDIRK SLQVSRHGSQ DKTKVLKRRV LDHYLYQGND LGISFAEDTI GIKLWTPAAG
     KVELLTYDSY TSENFEVDKL SPDTITEMDY DSDTGIYYTE LNKEFNENKF YLFRLTFGDQ
     VKYAVDPYAV AVGINGKMGA LVDINAPDTK PAGFEMDSKP ALAEPEDSIL YEMHIRDFTI
     NSDWGGKPEH AGKYLGLIEA GTKYQANGQS VSTGLDHLKE LGITHVHLLP TYDFVSTDES
     RPAPYDDQSP YEQASQRNWG YDPLNYNVPE GSYATNAADP KVRIKEYRQM VMGLHQAGIR
     VVKDVVYNHM AGMENMNNIA EGYYFRTWEE GTYSNDSGCG NAIESEHLMV RKFIVDSCNH
     WVENYNIDGL RFDLMAILDT TTMNQVKQQV RQKDNSILVY GEPWMADRSP LPWDRRTEKN
     KGLSFFNDTY RDALRGNNSP SKGYVTGEMT TNLTNVLRGL KAEDAGDPEE IINYVEAHDN
     YAIWDQVEKS ELGTINGQFR LNIPTNAFDD WRVDKAVLAN GFVLLSQGIP FYQGGSEILR
     TKQGDHNSYK SNDAVNDYDW ADKAEFKEVF EYYQGLIQIR KAQSLLRLTS KAKITAHQEV
     NRLNDRDDMI YQYLHDNPVD GEWKNMVILY NASNQEQPIT WLPGSQSAWK VAADDQGVYM
     DLPEADRRVV EKQGSQFAFK MAANSLMILY SFEEAVAPAN IHWHYLFADQ SRDYMSPLEP
     GIDDEITVRF RSKAGELTAA ELHYYVEGDP QVKVVAMREA AEDFYTSRGY DKNKLTFYEA
     TIPAGAANKY YHFKAINQVA ADNVKVAWIG AGEGEDHRGI SNQQLAQGFP IVPGYKTSKW
     SKESIFYQIM VDRFRDGDSQ NNKVKYDFAK NGDRPELSAW GSEIYKGTES DGIWNNQFFG
     GDLIGVKEAI PYLKNTLGVD ALYLMPIFQS DSDHKYDNDT YEYIDANFGG NLALAELGAD
     LKGNGLNYIL DGAFNHSSSS GQLFKEHRDF FFKGKWQDEN GVEYDHYPWH QKYFNFAKLD
     YSQAKTKDYI YAGDEAIAKR YLKAPYYAGG WRLDAAEDVS EIARDYKENE IIDPVQKASN
     LKIWQDFAHQ VRTADKDAFI LGEYWGNENH WYYGKAWDGK MNYGGFYLPF IENQSKNPWL
     GKHSLDNKGE MSVADIAKFT RNYMKDFPYA TILSSTNSLS THDKPRFLNV DYVGQDNTAM
     MVLAQTLQMT TPGIPLIYYG DEIGSFGKGD GSDPYNRQTF NWNDDQWNYQ ILNNYRKLIA
     ARKQNKDAFV YGAFEEVQSH HHQKYVVYAR YAGDQKAIVI LNNNGSNGSR IITLQDMDRF
     GLAEGTKLVD IFTGEQFMAE GNALKINSQD MSARCLVLES NYTLVEDLNA TFDVNTVLAD
     GKDQRHQLTA PLTPVYQKTE DGKVTVTYDL IDQTGVKGVL VRAVSRDDSR ELAKVEMPKT
     EKRVVFDNLP ADFKLVIKTV ADRDEKSGQV GDKYQDSGYV EVALKTENTP SDPNPGNPQD
     PGQPNDPNPG NPQDPGQPND PNPGNPQQPG NNQQPSTPGS FKPADNSGSD KIQSDLPEKP
     QMVIKNGKTY AEISLKSKEH KEAEIKLSKT GLQEILSKEA EGLKIQTPMA EVHLTKGLLQ
     KIQTASNEQT QITLKQYAKS DVVSQLKSIQ VKTDLLEIRI ENETSQKVWP QKEKIYVSIP
     YLLKAGEDKN QLLAFGLGKD GQITEIAASI YDAQRNRMIV AISPEMKIGV ASKSVSGSRF
     TDTENHYAKA EIDFVSARGL MQGVGNGRFA AQNQMDRAML VAVLGRLAGI DPADYQTSVF
     SDVPAGAYYA PYVTWAYQAG LVKGIGLNQY APTMNLTREQ TAVILAGFIE KYGYQLPVQQ
     TAAFTDADTI SDYAKSSVQA LQEAGIVKGK GANFDAKAEI SRAEISIMLK RLIELQMLQI
     QF
//
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