ID A0A2C1L087_9BACI Unreviewed; 713 AA.
AC A0A2C1L087;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
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:PGT91164.1};
GN ORFNames=COD11_01390 {ECO:0000313|EMBL:PGT91164.1};
OS Bacillus sp. AFS040349.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2033502 {ECO:0000313|EMBL:PGT91164.1, ECO:0000313|Proteomes:UP000222674};
RN [1] {ECO:0000313|EMBL:PGT91164.1, ECO:0000313|Proteomes:UP000222674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AFS040349 {ECO:0000313|EMBL:PGT91164.1,
RC ECO:0000313|Proteomes:UP000222674};
RG Agbiome Team Llc;
RA Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA Shank E.A., Bowers A.;
RT "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT roles of natural products in bacterial physiology.";
RL Submitted (SEP-2017) 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:PGT91164.1}.
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DR EMBL; NUMC01000007; PGT91164.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C1L087; -.
DR OrthoDB; 9761875at2; -.
DR Proteomes; UP000222674; 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; 2.60.40.2320; -; 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; IPR049117; pulA_all-beta.
DR InterPro; IPR040697; PulA_N1.
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; 2.
DR Pfam; PF02922; CBM_48; 1.
DR Pfam; PF21653; pulA_all-beta; 1.
DR Pfam; PF17999; PulA_N1; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF81296; E set domains; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000222674}.
FT DOMAIN 226..614
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 713 AA; 82200 MW; 03C679B9B6229D81 CRC64;
MGVLIMLSIN RRFQAFLDKM NEIAVIMPKE FDSENKTFFI KIDQNHEALS IVEKIDIGKQ
IKYVCSLSNP LSFGKTYIIS DEDGLETDLQ IGAVIRSDEF DKKFYYDGND LGANYTKEKT
EWKVWAPTAT IVKLRIYQSD GTQVDNFHMI RCEKGTWSIT LDGDFEGYYY TFLACINLVW
NEAVDPYARA VSINGEYGII IDQSLTNVPI IIPPALNQKT DTIIYEVHVR DFSIHENSGM
KNKGQYDAWT ELNTKNSQGD STGISYLKEL GVTHIELLPV NDFEEVDEQK PFEAYNWGYN
PLHYFAPEGS YSAAPENPYK RIIELKTLIQ SLHKQNLRVI IDVVFNHVYS KENSSFEKLL
PGYYFRHDEN GMPSNGTGVG NDLASERLMV KKFIADCVKY WMNEFDIDGF RFDLMGILDV
KTMNEVQKEV LEIKEDAILL GEGWDLLTPL PYVEKAIIPN AHKLPTISFF NDQFRDVIKG
STFSVHDRGF VYENLDTLEQ MKALITGSPT MFHEPHQSIN YVESHDNHTM WDRFLTFADA
ESEEIRKARH RLATSIVLLS QGIPFLHGGQ EFFRTKNGVE NSYNSPDEIN HLNWDERSQQ
KENVEYIKGL IKLRKLHGGF RLSSQELINK HVYFNDDPHL LSYEMENVGA YGPWERIVVI
HHPQCNKSYQ FKLPGNKGWK QIVSPSSILL DQPIDVDNKI EIREIGTYVF CKN
//
