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
//