ID A0A2V3WVN7_9BACI Unreviewed; 2174 AA.
AC A0A2V3WVN7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-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 ORFNames=DES38_101248 {ECO:0000313|EMBL:PXW93162.1};
OS Streptohalobacillus salinus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Streptohalobacillus.
OX NCBI_TaxID=621096 {ECO:0000313|EMBL:PXW93162.1, ECO:0000313|Proteomes:UP000247922};
RN [1] {ECO:0000313|EMBL:PXW93162.1, ECO:0000313|Proteomes:UP000247922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22440 {ECO:0000313|EMBL:PXW93162.1,
RC ECO:0000313|Proteomes:UP000247922};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061}.
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:PXW93162.1}.
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DR EMBL; QJJR01000001; PXW93162.1; -; Genomic_DNA.
DR OrthoDB; 9761875at2; -.
DR Proteomes; UP000247922; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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; cd10315; CBM41_pullulanase; 4.
DR CDD; cd02860; E_set_Pullulanase; 1.
DR Gene3D; 2.60.40.1110; -; 4.
DR Gene3D; 2.60.40.1220; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR005323; CBM41_pullulanase.
DR InterPro; IPR014755; Cu-Rt/internalin_Ig-like.
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; IPR045857; O16G_dom_2.
DR InterPro; IPR011838; Pullulan_Gpos.
DR InterPro; IPR040806; SpuA_C.
DR NCBIfam; TIGR02102; pullulan_Gpos; 1.
DR PANTHER; PTHR43002; GLYCOGEN DEBRANCHING ENZYME; 1.
DR PANTHER; PTHR43002:SF11; PULLULANASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF00128; Alpha-amylase; 3.
DR Pfam; PF02922; CBM_48; 1.
DR Pfam; PF03714; PUD; 4.
DR Pfam; PF18033; SpuA_C; 1.
DR SMART; SM00642; Aamy; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 4.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000247922};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 2147..2168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 393..770
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 1337..1737
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1879..1928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2086..2141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1902..1921
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2099..2114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2174 AA; 242336 MW; 7693FB474FF9F2CC CRC64;
MNQLKRIKPL VSLLMVWALL ISTILTALPL SVVAETGSDA PPAIEENHLR IHYEHTGTTD
EQLYLWSWGD VVENNEGDWP LGNAFKVSDD ASYNMYTDIE LKSEANEIGV QVVKAASENE
KVVDDTTIEI IAPEMNEVWI SAEGDVSLYQ PVDFAEPTVR IYYQETEAAY TDPGLWFWGD
VVTEPTEWAE DAYAFNEGTS SKYGNYIDIK LTDGPASIGM LIVDKALADG EENHQQSDNI
NFDDLENHQQ IFLQEGHLEA YTNPYYISSE EETEPLPEET PGEAEITATA AVSRAFNYDE
HAILSVLIDN QSALTIQSIR ADVSALGGTS ALEISPELNE VVLSVQEGIA TGEKDIPITI
VDSAGGTYTT TATAEITEKT EASRDWDESI IYFMLTDRFF DGDETNNNPY DLAYNQADNP
RGTYQGGDFE GVTAKLDYLD ELGVNTIWVT PIVENVGHDV EALSDNGSYY AYHGYWAENF
ETLNPHLGTL AEFHTLIDEA AARDIDIMVD VVLNHAGYGM NADLTEGMPE GHPTAEDLAR
FDGMLREDSG SGDLKMSLSG LPDFVTEDQQ VREDLVEWQS AWLEKSTTAN GNRIASYRVD
TVKHVDQTTW QLFKNELVKL DPSFKLIGEH WGANYQEDGG HFNDGTMDSL LDFGFKTYAE
GFVNGHLSAN ETILIERNAS LTNTYTLGQF LGSHDENGFL YEIDNDVDKY KVAASLQLTA
KGQPVIYYGE EIGQTGENNW PVYDNRYDFD WEAVESSDIH DHYQTVLSFR NEFSKVLAKG
NRETVVVNDE LGHLISKRSH NGTSVYLGFN VTDQPQEISL NTSTEEVIVT DHYSGDVFSA
TATDEGAAVT VTIPAMADGG TVLLSTEGGE LLSVTDTPID EEVNENEVTP VEKGYFRLHF
RQLDRFDLSS SGLWIWEDVA TSSENWPLGA INLEEAAVQT EFGHYIDVEI KEDASQIGFL
INNASGDNLT GDQFVDVLSP DMNEAWITED FDVYPYQPVN LDGKVRINYH REDGDYQGWA
LWTWGDVVEP TDGWPDGAHD FVSGDYGVFY DLPLIEDASQ INFLTLNKES GNQSSDMSFG
ELEQSQIFIR DGDVNVYTNP YFVTEEGLTN ADFTALDTIE LSYSLVGDWT KDDLIEAIEV
TTKEGDLVSI SDLTIKKETN KISLHGDFKI DDAPYTVTHL GREQAAKAGW RLKDSLYGYD
GDLGLTALSN GEATIKVWSP SADDVALVLY DKDNPEVMID KFKMQRTDQG VYAITLTDEV
TGIENHEGYF YHFEVTRGEE TVLAIDPYAR SMAQWSSEVA VDSVGKAAIV DPSTIGPTLD
YADIDGFEHR EDAIIYEVHV RDFTSDPSIE AELNAQFGTF SAFREKLDYI ESLGVTHVQL
LPVMSYYFSN EFANDQRLLE YSSTDNNYNW GYDPHSYFSL TGMYSEDPSD PAKRIEEFKA
LIADIHSRGM GVILDVVYNH TARVEIFEDL EPNYYHFMDE ELEAKTSFGG GRLGTTHKMS
RRILVDSITY WVEQFKVDGF RFDMMGDHDA ASIQMAYDKA KQLNPNILMI GEGWRTFAGD
DDDPNVQPAD QDWMKDTNSV GSFSDEFRNE LKSGFGSEGQ PRFLTGGARN VEQIFNNLTA
NPGNFTATHP GDVVPYIAAH DNLTLHDVIA QSIKKDPKDY EEEIHQRIRL GNLMVLISQG
TPFIHAGQEF GRTKQFKDPD FINEVEVAPY KSTFMTDASG EPFEFPYFIH DSYDSTDVIN
NIEWDKATNR EAYPVHTMTQ RYTSGLIHLR RSTDAFRKAT MAEIESDVKM INAPEINTTD
LVVAYQATDS KGDTYHVFIN ADSKARALTV ETNYLAGDVL VDGQQAGTDV IEAPVGVSVT
ENTVTLAPLT AFVVRINADP SSQPDEDHAE EPPNTSPVIP DEEETTEIDD DNLDVDEETD
GTIVDGNDKT DLSIKPDLFE KLTDKAQLKM RGKANTFSMN FPLSNVLKRA KDQNQTIRAI
VKQIAKAEAP KKKGVEPLSD AYDLSIFIGD HYVDEAFETP VELRFTVNSE AVTDQGDIRL
VYINNDGEFI YYPIDRYNAE TGEVIAFVTH FSQYMIAMVN DAVVDAPPVE RPDSEPVEGE
TSDTPSQSTE DTSVDTEEGV VESEVAPVLE DETTSTDDTL PDTAHSFYRN ILVGLLLIVV
AAVGIIGTRR KESK
//
