ID A0A011Q6R8_9LACT Unreviewed; 661 AA.
AC A0A011Q6R8;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=ADIAL_1483 {ECO:0000313|EMBL:EXJ23021.1};
OS Alkalibacterium sp. AK22.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Alkalibacterium.
OX NCBI_TaxID=1229520 {ECO:0000313|EMBL:EXJ23021.1, ECO:0000313|Proteomes:UP000020164};
RN [1] {ECO:0000313|EMBL:EXJ23021.1, ECO:0000313|Proteomes:UP000020164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK22 {ECO:0000313|Proteomes:UP000020164};
RA Singh A., Pinnaka A.K.;
RL Submitted (JAN-2014) 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:EXJ23021.1}.
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DR EMBL; JANL01000035; EXJ23021.1; -; Genomic_DNA.
DR RefSeq; WP_034301938.1; NZ_JANL01000035.1.
DR AlphaFoldDB; A0A011Q6R8; -.
DR STRING; 1229520.ADIAL_1483; -.
DR PATRIC; fig|1229520.3.peg.1448; -.
DR eggNOG; COG1523; Bacteria.
DR OrthoDB; 9761875at2; -.
DR Proteomes; UP000020164; 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; 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; 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; 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 SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF81296; E set domains; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000313|EMBL:EXJ23021.1};
KW Hydrolase {ECO:0000313|EMBL:EXJ23021.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000020164}.
FT DOMAIN 172..559
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 661 AA; 74777 MW; 897C33E9442D0F44 CRC64;
MDIKQPLELR IPYLEDRLYE KNDLGLNYHQ NYSTFKVWSP LAKEAWLCLY DSADALDPVR
KLRMTARENV WSIKVSDDLN GYFYTYVFVH DKKEVETADL YSTAVGLNGD RSAIINLSDT
DPEGWQEDYF DQVDAITEAI IYEVHVEDFS SDEAADFNPD FRGKYLAFTE TGVTVEGVSD
QPAGLDYLTD LGINYVHVLP AFDYQNDEES NAYNWGYDPK NYMVPEGKYA TDPADPTARI
REFKAMVASL HARGIGVILD VVYNHTFDLG RSAFQKTVPD YYYRQNQDGS PANGSGCGNE
TASERRMMRK YIIDSLMYWI EEYHIDGIRF DLMGLHDVQT MNLLRETLNA NGHEKVLIYG
EPWNAGSVAI FEPNKPADKY HVGELADGIA IFNDEFRDAI KGPVFDAGQG AFLQGANGRE
GSAYSNSDLI ASILANTQQH VGRFSLPQEK NWARTPAQVV TYASAHDNLT LYDKLVASRT
DRSSYGRNVE LIQLNKINAA LLFTSLGGTF FQAGEEFART KAGDENSYRS SININQLDWR
RAYDNKDLRN YYKGMIQIRR HYRPLQDRTN KTGDNITFSQ LRENVIAYTI PNTSGEGDWS
IMAVIANTSD HSDWVELKSS FPLPDEWTIL ANRHTAGTRS LGTVIGNLLL INSKEVLVLV
A
//
