ID A0A2N0UU23_9FIRM Unreviewed; 1059 AA. AC A0A2N0UU23; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 27-MAR-2024, entry version 21. 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_2 {ECO:0000313|EMBL:PKD30504.1}; GN ORFNames=RBL236_00821 {ECO:0000313|EMBL:PKD30504.1}; OS Ruminococcus bromii. OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae; OC Ruminococcus. OX NCBI_TaxID=40518 {ECO:0000313|EMBL:PKD30504.1, ECO:0000313|Proteomes:UP000233570}; RN [1] {ECO:0000313|EMBL:PKD30504.1, ECO:0000313|Proteomes:UP000233570} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L2-36 {ECO:0000313|EMBL:PKD30504.1, RC ECO:0000313|Proteomes:UP000233570}; RX PubMed=29159997; RA Mukhopadhya I., Morais S., Laverde-Gomez J., Sheridan P.O., Walker A.W., RA Kelly W., Klieve A.V., Ouwerkerk D., Duncan S.H., Louis P., Koropatkin N., RA Cockburn D., Kibler R., Cooper P.J., Sandoval C., Crost E., Juge N., RA Bayer E.A., Flint H.J.; RT "Sporulation capability and amylosome conservation among diverse human RT colonic and rumen isolates of the keystone starch-degrader Ruminococcus RT bromii."; RL Environ. Microbiol. 0:0-0(2017). RN [2] {ECO:0007829|PDB:7LSA, ECO:0007829|PDB:7LSR} RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 1-797 IN COMPLEX WITH CA(2+). RX PubMed=34186214; DOI=10.1016/j.jsb.2021.107765; RA Cockburn D.W., Kibler R., Brown H.A., Duvall R., Morais S., Bayer E., RA Koropatkin N.M.; RT "Structure and substrate recognition by the Ruminococcus bromii amylosome RT pullulanases."; RL J. Struct. Biol. 213:107765-107765(2021). 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:PKD30504.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; NPHY01000011; PKD30504.1; -; Genomic_DNA. DR PDB; 7LSA; X-ray; 1.76 A; A=1-797. DR PDB; 7LSR; X-ray; 2.42 A; A=1-797. DR PDB; 7LST; X-ray; 2.05 A; A=1-800. DR PDB; 7LSU; X-ray; 1.95 A; A=1-799. DR AlphaFoldDB; A0A2N0UU23; -. DR SMR; A0A2N0UU23; -. DR Proteomes; UP000233570; Unassembled WGS sequence. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. DR GO; GO:0051060; F:pullulanase activity; IEA:UniProtKB-EC. DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW. DR CDD; cd11341; AmyAc_Pullulanase_LD-like; 1. DR CDD; cd14256; Dockerin_I; 1. DR CDD; cd02860; E_set_Pullulanase; 1. DR Gene3D; 1.10.1330.10; Dockerin domain; 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; 2. DR Gene3D; 3.10.20.320; Putative peptidoglycan bound protein (lpxtg motif); 2. DR InterPro; IPR031965; CBM26. DR InterPro; IPR002105; Dockerin_1_rpt. DR InterPro; IPR016134; Dockerin_dom. DR InterPro; IPR036439; Dockerin_dom_sf. 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; IPR009459; MucBP_dom. 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; PF16738; CBM26; 1. DR Pfam; PF02922; CBM_48; 1. DR Pfam; PF00404; Dockerin_1; 1. DR Pfam; PF06458; MucBP; 2. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF81296; E set domains; 1. DR SUPFAM; SSF63446; Type I dockerin domain; 1. DR PROSITE; PS51766; DOCKERIN; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:7LSA, ECO:0007829|PDB:7LSR}; KW Calcium {ECO:0007829|PDB:7LSA, ECO:0007829|PDB:7LSR}; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326}; KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:PKD30504.1}; KW Hydrolase {ECO:0000313|EMBL:PKD30504.1}; KW Metal-binding {ECO:0007829|PDB:7LSA, ECO:0007829|PDB:7LSR}; KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}. FT SIGNAL 1..27 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 28..1059 FT /note="pullulanase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5014903365" FT DOMAIN 798..861 FT /note="Dockerin" FT /evidence="ECO:0000259|PROSITE:PS51766" FT BINDING 262 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0007829|PDB:7LSA, ECO:0007829|PDB:7LSR" FT BINDING 263 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0007829|PDB:7LSA, ECO:0007829|PDB:7LSR" FT BINDING 268 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0007829|PDB:7LSA, ECO:0007829|PDB:7LSR" FT BINDING 288 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0007829|PDB:7LSA, ECO:0007829|PDB:7LSR" SQ SEQUENCE 1059 AA; 116219 MW; FF6E3BFE1731A041 CRC64; MRTTKKIVSA VLAACMLAST AVVSSFAATA DDSSAVSSDY ARDNSYTKAA EDIDAQYAYS GNDLGVTYTK DATTFKVWSP TATGVKLNIF TKGSDDEQGA SKVASYTLEK MLVDGEWNGV WTITLVGEWK DYYYTYSVTT TDTTHIGSDA TKTYETQDVY STATGVNGKR SMIVDLDETD PEGWSNDSHV LLDKSTKSSV WELHIKDFSY DKASGVSDAN RGKYLAFTEN GTTLNGEGKV STCIDYLKEL GVTTVQLNPF YDFQSVNEAG DDSQFNWGYD PVNYNVPEGS YSSNPYDGKV RIKECKEMIK ALHDAGISVV MDVVYNHTYS TDSCFQYTVP NYYYRMKTTG AFSDGSGCGN EGATERAMYR QYVIDSLKYW VNEYHVDGFR FDLMGLMDVE TMNMAREALD QIDPRITMWG EGWAGGDSYH PTNTCSGTKF YPATQANASR LSDRIAIFND GIRDGIKGSA MDISDVGFIQ GSKSSAKGVS YGVRANSSGT YKWKAQAPSQ CVTYDACHDN ATLYDQIIAS TGLADYGERN SEAVKMNRLA SAIIYTSQGI SFTLAGEEMA RSKDGDTNSY KSAANLNMIK WQNVVDYADV VSYYKGMMQI KSAFSPLTAM DNSYADKYTF TKKVSASTNQ ISFTIQNDVE GEWNKMAVIY NNATTAADVT LSDTSVTDWV VIANGETAGL DSLGEVTGST FTVPARSAIV AVDKAGYESA GIHSSKGKVK VNYVYEATGE KLEDSVILQG SVGSGYVTVP SAVIPDTYIV SRIGGNAEGK YTSDMQEVTY YYTDYIPESL KNADFNGDGE INVIDATLLQ KYIAKLETPT VDESTLDLNY DGTFNIEDST MIMKYVARIP VSSGKVTVNY YYTDADGKQQ KLTDSIVFAG RAGSTYKSTA FKVVGYAVDP DRMPENQSGL IPYGEAEVNY YYIASSLDIK LHVKHNGSLT WTPYLWIWGS DLKGKDSGNF MSEWPGDPMT EGENGWFDYS FTYKGAGTYN VIVSDNATNQ TIDYKGFVDN EMWIVIDDSA VMGSTYLTFY TDNPDTNPNA PIAEQVTLG //