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Database: UniProt
Entry: Q6LIJ2_PHOPR
LinkDB: Q6LIJ2_PHOPR
Original site: Q6LIJ2_PHOPR 
ID   Q6LIJ2_PHOPR            Unreviewed;      1110 AA.
AC   Q6LIJ2;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   SubName: Full=Pullulanase {ECO:0000313|EMBL:CAG22888.1};
GN   Name=PULA {ECO:0000313|EMBL:CAG22888.1};
GN   OrderedLocusNames=PBPRB1016 {ECO:0000313|EMBL:CAG22888.1};
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386 {ECO:0000313|EMBL:CAG22888.1, ECO:0000313|Proteomes:UP000000593};
RN   [1] {ECO:0000313|Proteomes:UP000000593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9 {ECO:0000313|Proteomes:UP000000593};
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061}.
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DR   EMBL; CR378678; CAG22888.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6LIJ2; -.
DR   STRING; 298386.PBPRB1016; -.
DR   KEGG; ppr:PBPRB1016; -.
DR   eggNOG; COG1523; Bacteria.
DR   HOGENOM; CLU_004744_5_0_6; -.
DR   Proteomes; UP000000593; Chromosome 2.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0051060; F:pullulanase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11341; AmyAc_Pullulanase_LD-like; 1.
DR   CDD; cd10315; CBM41_pullulanase; 1.
DR   CDD; cd02860; E_set_Pullulanase; 1.
DR   Gene3D; 2.60.40.1110; -; 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   Gene3D; 2.60.40.1130; Rab geranylgeranyltransferase alpha-subunit, insert domain; 1.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR005323; CBM41_pullulanase.
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; IPR011839; Pullul_strch.
DR   InterPro; IPR024561; Pullul_strch_C.
DR   InterPro; IPR041111; Pullulanase_Ins.
DR   InterPro; IPR040671; Pullulanase_N2.
DR   NCBIfam; TIGR02103; pullul_strch; 1.
DR   PANTHER; PTHR43002; GLYCOGEN DEBRANCHING ENZYME; 1.
DR   PANTHER; PTHR43002:SF11; PULLULANASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF02922; CBM_48; 1.
DR   Pfam; PF03714; PUD; 1.
DR   Pfam; PF11852; Pullul_strch_C; 1.
DR   Pfam; PF18494; Pullulanase_Ins; 1.
DR   Pfam; PF17967; Pullulanase_N2; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF81296; E set domains; 2.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000593};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1110
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004276080"
FT   DOMAIN          95..185
FT                   /note="Pullulanase carbohydrate-binding module 41"
FT                   /evidence="ECO:0000259|Pfam:PF03714"
FT   DOMAIN          204..315
FT                   /note="Pullulanase N2"
FT                   /evidence="ECO:0000259|Pfam:PF17967"
FT   DOMAIN          326..410
FT                   /note="Glycoside hydrolase family 13 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02922"
FT   DOMAIN          508..581
FT                   /note="Pullulanase Ins"
FT                   /evidence="ECO:0000259|Pfam:PF18494"
FT   DOMAIN          935..1095
FT                   /note="Alpha-1,6-glucosidases pullulanase-type C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11852"
SQ   SEQUENCE   1110 AA;  120847 MW;  FEF0FE4B10DCEA1E CRC64;
     MNFKLSTIAK LMFPLLSTAA IVGCNSSSDS SGDSGNGYFD TTNPPAININ LPVTDGPVAK
     LPAGGAVEEP IKAANGEAVL YFVEKSDSAV AKSTADYLNY SLHIWNNDKC DRADDELLVG
     WDDESNKPVG ADQYGPYWKL PLTAGSTNCI NLIVRDNNKQ NLLGADGSIN FDDITDRTAS
     IVAGSGTSVD RRESAFVSIS GIANASAHLV DQNTLLWDGA EGADEVRLYV SLAADIEPKG
     DAYAYENDYI VLDSGTMSAD AIAKFPQLVG KPAFSVDSAI NMRPVMKAEM AVIAVDKDGN
     VLGGTKVQPA GAYDDMFAQY ARNAELGAVL AGSEATFQVW APSAQNIVTV LYDANKKELG
     RLQMDFDEDS GVWFLKTDKA PSGTFYRYLV LVVHPVTGDV EEYEVTDPYS LSLSMNSEYS
     QVIDLDDPAL KPDGWDSLER PFKQDNPSKF VIYESHVRDF SAQDASTPEA VRGKFEAFTQ
     DDTVPVRHLK SLQENGVTHL QLLPIFDIAT INEDPDQVAN INEPFSKLCD VNSDVKTSSF
     KNDCSSGLTI AEILEREQGN DTAANPSVQE LNRLVSATDS FNWGYDPLHY TVPEGSYSTN
     PDGKQRILEM REMVKSIKTD IGMNVVMDVV YNHTNSAGPE SETSVLDKIV PWYYNRLNPV
     TGSVENSTCC SNTAPERTMM GKLIKDSLVV WSRDYKIDSF RFDLMGHHPL AQIQESLAAV
     KNVDPNTYFY GEGWNFGEVE NDRLFVQATQ PNLGGTGIGS FSDRLRDAVR GGGPFDGGDG
     LRENQGFGNG AFVQPNDITT TDKETALHLA DLTRLGMAGN LESFVMIDST GSKVRGDQVD
     YNGQPAGYAV DPSEVQNYVS KHDNQTLWDN NQYKIPYDVT SATRVRMQTV SLSTAMLGQG
     VPFLHMGSEL LRSKSMQRDS YDSGDWFNKV DFTLQDNNWN KGLPRKDKDG DNYAIITEVI
     DGSGTNAQPS PKDMADMVSF YQELANLRQS YPLITLGTGE EVNARVDFHN TGTTQEAGLI
     VMSIDNGTGS GADLDSTLDA MVVVINATPT VKTFDIKQTG FTVSEKHTTA LATGALVADE
     TKLTVPAWTP VVFVQKRSGE RGVGLPVSTK
//
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