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Database: UniProt
Entry: Q6NJP1_CORDI
LinkDB: Q6NJP1_CORDI
Original site: Q6NJP1_CORDI 
ID   Q6NJP1_CORDI            Unreviewed;      2578 AA.
AC   Q6NJP1;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 104.
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   OrderedLocusNames=DIP0357 {ECO:0000313|EMBL:CAE48862.1};
OS   Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS   gravis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=257309 {ECO:0000313|EMBL:CAE48862.1, ECO:0000313|Proteomes:UP000002198};
RN   [1] {ECO:0000313|EMBL:CAE48862.1, ECO:0000313|Proteomes:UP000002198}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis
RC   {ECO:0000313|Proteomes:UP000002198};
RX   PubMed=14602910; DOI=10.1093/nar/gkg874;
RA   Cerdeno-Tarraga A.M., Efstratiou A., Dover L.G., Holden M.T.G., Pallen M.,
RA   Bentley S.D., Besra G.S., Churcher C., James K.D., De Zoysa A.,
RA   Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S.,
RA   Jagels K., Moule S., Quail M.A., Rabbinowitsch E., Rutherford K.,
RA   Thomson N.R., Unwin L., Whitehead S., Barrell B.G.Parkhill.J.;
RT   "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT   NCTC13129.";
RL   Nucleic Acids Res. 31:6516-6523(2003).
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}.
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DR   EMBL; BX248354; CAE48862.1; -; Genomic_DNA.
DR   RefSeq; WP_010934239.1; NC_002935.2.
DR   STRING; 257309.DIP0357; -.
DR   KEGG; cdi:DIP0357; -.
DR   HOGENOM; CLU_000910_0_0_11; -.
DR   OMA; TREQFYF; -.
DR   Proteomes; UP000002198; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; 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; 5.
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; IPR024561; Pullul_strch_C.
DR   InterPro; IPR040671; Pullulanase_N2.
DR   InterPro; IPR044055; RibLong.
DR   NCBIfam; NF038186; YPDG_rpt; 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   Pfam; PF18957; RibLong; 4.
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   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002198};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        2548..2569
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          170..627
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          180..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..199
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2578 AA;  283245 MW;  0185EA1731C17385 CRC64;
     MRDSALPRYF RALVAVISAI SLVGVGLHAT QPTARADEEL APAVVAGTFQ KNLGCSKEWE
     ESCDKTRMKR KGNLYATTLK IPEGDWKFKV VLNGDWGTSY GAPGFDENNI PLKLTKDTEL
     EFSFDPLSHR IGLKPVGLDD EKLKTYDDSK DKDIVGAPFK HSAAGKNFYF VLTDRFQNGN
     PENDRGGAKD GDKNDHGFDP TDKAYYHGGD IEGLIKQLDY IKNLGTTALW LTPSFKNRAV
     QCGHDPKDCS SGYHGYWITD FTQIDPHLGS NDDLKRLIEE AHNKGIKVYF DIVANHTADL
     IQLAGGNQYI SEDQQKYKDV DGKEFLLKDY AGKKEFPELN DFSFPYKPIR KPEDNIIVPK
     ELNDVHLYHN RGNNTWEGES VIHGDFEGLD DLMTEHPKVV SHMIEAYNKW AGFGLDGFRI
     DSVKHVNMEF WKEWTEAVKK HAKESRAGEK EDFFMFGEVF NGTAESLSPF VRDTQMDAAL
     DFAFHYKALD FAKGQSTQGL HDLFYSDDWY TTTRSDATNL PTFLGNHDVG RIGYLLRDND
     DKVQRDVLAH QLMFLTRGQP VVYYGDEQGF AGTGDGKDKQ ARQDMFGTQV DEFKNEQDIY
     GKQLGSDNHF KESGELYGKI KQLAELRTAN KALATGAQIE RWETPGPGIY AFSRVDRDEK
     QEYLVALNNS HLEQTATPAP LTPNASFTKI YGEGPDKISP NLDGTVNLKL PRLSAVVYKV
     ESNQKVSGAV DGTGLSVKGQ ALKDNAPIMT NIGGKAWSET SFAWRELGTE EWKKLGTDTG
     QNARVFHDVR DLKPGTIVEY RTVTVDADNN KTASTGWGVV GVDLGVDTAA LLAPSAVVAG
     DFTKDLGCTG GDQGNWDPAC AKTELKSVGG TDWHTVKLNL KAGEHQYKIA VAGSWNENYG
     QEKDGDRPND RGYHNGKNVK FNLDREQEVQ FFYNPVTNEF FNSVEHGVIT LPGTMGGALN
     CPKNDQKSDE HGNWGPACLA TLMTKTGDHI YEFSSPKVPT PGNYDVKVAY GLEWGNDWGP
     DGHKTQRNYD VKITDSGILH YRWDENKHEL TWNITERSSL DLQDTFAHWL DDRTIAVPRS
     QLRDASPSDV EGLLVSVSDG KPSIKSGKGA SSQADAKIEE QKLHYVGQIG GDLLARNPHL
     DGMVTFRFKD EVQKDKAREL LQGGLGFAVV KKKEQEPVSF TGVQIPGVLD AHYAADARDA
     QLGVHWKGDK PTVSLWAPTA KNVKLKLFGE EGSLGNGEDH KMDYDKTTGV WSVEGKPDWK
     NHAYQFEVEV YAPSTHKVEH NLTTDPYSVG LSMDSKYSVM LNLNDPELKP ADWGKAMDPI
     DPVDRMIYEL HVRDFSASDK SMDQQYRGKY KAFTQSGSKS VMHLKELADA GLNSVHLLPT
     NDIATIPEDP AKAKTPAITS TGAADTQQQE AVAAVQKEDA FNWGYDPYHY MAPEGSYATK
     PDAKTRVKEY REMVKALNGM GLHVVSDQVY NHAFQGQQDE KSVLDKVVPG YYHRLMLDGK
     IANSTCCANL ATEHVMMEKL MTDSVKSWAK NYHIDGFRFD LMGHHSAANM INVQTELSEL
     TVEKDDIDGS SIYLYGEGWN FGEVENNQRF IQATQENLAG TGIGTFNDGL RNGVHGHEGR
     TQGFGTGLAM EGNGTDQKDQ GHLRHLTDIV RVGMAGNLQD FKFNSKDGYK RGGDIWLDGK
     RIGYGLMPQD TVNYVDAHDN QTLYDLSVLQ LPQSLSMDDR VRMNTVQLAT VALGQSPAFW
     HAGTEIMRSK SLDRDSYNSG DHFNKLDLSM QEHNFGVGLP IAEKNDKQWE LYKGFLNDEH
     LKAKPEDLKK ANDMAKELMT LRKDNPLMRL GDVDQIQEKV TFPANGPDAQ PGLIVMNIDD
     TKGEDRDAKR DGILIVINSS PKQIEQTINE LEGLDFTLEK TLAEGVDKET QKGSTWNKAE
     KKLTIPARTV AVFERTQNEA AHHDPQYPET KVFKDATEDV KVEGPKDMPE TAKYSIDPAV
     DGVSVDEKTG ALTVKPTAIK EDGLVVTVTV KYSDGSEDRA VAKFVTDTSI ASMYDPTYEE
     TKAESADKKV TIKKPMSGEK SLPEDAHFTL EGESAKKATI DGFTGEITVE PLKDERRLEL
     DVKVTYADES VDMVKAVVVA GDTLADQHDP KYADTQMEKG TKTVIAAPEG MPENIKYELA
     EPQDGVTVRD DGSIEVTTDA ESLDIKVKVT YSDKSTDTAV AHVTTVAQTE QSVEVTPGTQ
     TLVDVPGNGD VTVTVPQNSG LKAEVAGNLV TLTSDGSVEG HVTVTYQVKD ADGKTTTGKI
     NVQVAKLAEA SWPKSASVAA GDSTVITPEG VDTLPYGTTL SVGSLPEWAT FDQTTGQLTL
     TADEDATDES TTATITVAYP DGLTKQYSVA LSVGAATETT ADQHDPQWES VVVNGDSVTS
     HGVDVPADAE VSVDKLPEGW TATVTGSDVE ITPAAGSPAG HVIALPVTVR YADGTTDTAV
     INVLTQPDWS TSNKAPKADS GMFYQAGPGA PAWVRVNNDG SMTWADNAPE GTHEIPVIVT
     KDGVHYLVTA SVNAPKKVVL DTEGSSSILG VVVAILAAGG IMALFALLFN CTWFKNCR
//
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