ID   A0A2N0UU23_9FIRM        Unreviewed;      1059 AA.
AC   A0A2N0UU23;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   20-JUN-2018, entry version 3.
DE   SubName: Full=Pullulanase {ECO:0000313|EMBL:PKD30504.1};
DE            EC=3.2.1.41 {ECO:0000313|EMBL:PKD30504.1};
GN   Name=pulA_2 {ECO:0000313|EMBL:PKD30504.1};
GN   ORFNames=RBL236_00821 {ECO:0000313|EMBL:PKD30504.1};
OS   Ruminococcus bromii.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
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.,
RA   Walker A.W., Kelly W., Klieve A.V., Ouwerkerk D., Duncan S.H.,
RA   Louis P., Koropatkin N., Cockburn D., Kibler R., Cooper P.J.,
RA   Sandoval C., Crost E., Juge N., 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
RT   Ruminococcus bromii.";
RL   Environ. Microbiol. 0:0-0(2017).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|SAAS:SAAS00964676}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:PKD30504.1}.
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DR   EMBL; NPHY01000011; PKD30504.1; -; Genomic_DNA.
DR   Proteomes; UP000233570; Unassembled WGS sequence.
DR   GO; GO:0051060; F:pullulanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.10; -; 2.
DR   Gene3D; 2.60.40.1180; -; 1.
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   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; SSF51445; 1.
DR   SUPFAM; SSF63446; SSF63446; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   TIGRFAMs; TIGR02104; pulA_typeI; 1.
DR   PROSITE; PS51766; DOCKERIN; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000233570};
KW   Glycosidase {ECO:0000313|EMBL:PKD30504.1};
KW   Hydrolase {ECO:0000313|EMBL:PKD30504.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     27       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        28   1059       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5014903365.
FT   DOMAIN      798    861       Dockerin. {ECO:0000259|PROSITE:PS51766}.
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
//