ID R7I2B2_9CLOT Unreviewed; 987 AA.
AC R7I2B2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=BN648_02132 {ECO:0000313|EMBL:CDE44642.1};
OS Clostridium sp. CAG:411.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262802 {ECO:0000313|EMBL:CDE44642.1, ECO:0000313|Proteomes:UP000018022};
RN [1] {ECO:0000313|EMBL:CDE44642.1, ECO:0000313|Proteomes:UP000018022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:411 {ECO:0000313|Proteomes:UP000018022};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDE44642.1}.
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DR EMBL; CBIY010000087; CDE44642.1; -; Genomic_DNA.
DR AlphaFoldDB; R7I2B2; -.
DR STRING; 1262802.BN648_02132; -.
DR Proteomes; UP000018022; Unassembled WGS sequence.
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; cd11341; AmyAc_Pullulanase_LD-like; 1.
DR CDD; cd02860; E_set_Pullulanase; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
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; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR InterPro; IPR011840; PulA_typeI.
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; 1.
DR Pfam; PF02922; CBM_48; 1.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00089; PKD; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000018022}.
FT DOMAIN 195..624
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 807..897
FT /note="PKD/Chitinase"
FT /evidence="ECO:0000259|SMART:SM00089"
FT DOMAIN 900..987
FT /note="PKD/Chitinase"
FT /evidence="ECO:0000259|SMART:SM00089"
SQ SEQUENCE 987 AA; 108959 MW; 3817C13C8E5D0B20 CRC64;
MKHGVAKRAL GVVMTSAMVA GTVGTVPLGN WNKSAVDTVL AAGQSAMYVD STDYYNAAYD
KENAYTGDDL GCTYTKEKTV FKVWSPEADK MTLNLYATGS DKEEGAKDLG NFSMKKTDKG
VWEYTYEGDL KNTYYTYRAM IDGMSYGETV DPYAKAAGVN GERGMVVDLD STDPSGWDTN
YKRTATNLSD IVVWEVHIRD FSIDVSSGVS AENRGKYKAF TESTTVNGEG KVSSCVDYLK
KMGVTHVQLL PMFDYGGIDE TKTTNELSDS NYNWGYNPVN YNVPEGSYSS NPYDGNTRIK
EMKQMIQALH DAGIKVIMDV VYNHTYETGT SCFSKLMPDY YYKLTTDSAG NVVYNDESGC
GNATRSGAAM YDKYMRDSLK YWVSEYNIDG FRFDLMGIHD AKTMNNIRKD MDDNFGNDTI
VLYGEGWTGG GYSKDSAYKE YCRNLDEGIG YFNDQIRDAI KGETGNEKVS QIGFAQQNYG
LDGTYTDHEK FPTSVFGGIM GSVGKNTSNW WMWRAYWADT SNRVLSYDSC HDNMTVWDKF
VQSMGVKDFS TTDNRLLNMS RMTAGYLLTS HGGTFLHAGE EFARTKNGNE NSYNAGDSDN
KLDWNRISSY GNLTDYYQGM IAIRKAFSGF RNILTETGDV VEENTASGFF NKVNGNNITN
IPEFTEVVEG KNENNQIQST VNSIGYYLSN DVANEWNQVA VLMNNTTTAK TAQLTATDGS
QEWVLVSDGK QASVTGIATS SGSAITVPGK SVVVAVPKKA FDSVKFTGED KIIPITEEDK
DEPIVSPEPT KEPEVTPAPV TPSAIKISKF TVTPTTVKNG SGTVKMSVKM AASTTDACEY
RFYVYKGDVL VKSSAWSEKD NFEWKATKAG TYTIVVRVRD TAGNMVSAEK TVSVFDKLTV
KSVKADKKVV KKGKNITFTV KATGGKTAYK YSFKVVKTSG KIVKKSNTIS SGKWIWKATQ
KGTYNVKVTV KDKFGATVTK TIKIVVK
//
