ID D4BLR9_BIFBR Unreviewed; 1708 AA.
AC D4BLR9;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=1,4-alpha-D-glucan glucanohydrolase {ECO:0000256|ARBA:ARBA00030238};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
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:EFE90257.1};
GN ORFNames=BIFBRE_03006 {ECO:0000313|EMBL:EFE90257.1};
OS Bifidobacterium breve DSM 20213 = JCM 1192.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=518634 {ECO:0000313|EMBL:EFE90257.1, ECO:0000313|Proteomes:UP000003191};
RN [1] {ECO:0000313|EMBL:EFE90257.1, ECO:0000313|Proteomes:UP000003191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20213 {ECO:0000313|EMBL:EFE90257.1,
RC ECO:0000313|Proteomes:UP000003191};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000256|ARBA:ARBA00000548};
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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:EFE90257.1}.
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DR EMBL; ACCG02000002; EFE90257.1; -; Genomic_DNA.
DR RefSeq; WP_003827986.1; NZ_JDUD01000003.1.
DR KEGG; bbrd:BBBR_0107; -.
DR PATRIC; fig|518634.20.peg.112; -.
DR HOGENOM; CLU_001641_2_2_11; -.
DR Proteomes; UP000003191; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051060; F:pullulanase activity; IEA:UniProtKB-EC.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR CDD; cd11341; AmyAc_Pullulanase_LD-like; 1.
DR CDD; cd10315; CBM41_pullulanase; 2.
DR CDD; cd02860; E_set_Pullulanase; 1.
DR Gene3D; 2.60.40.1110; -; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR005085; CBM25.
DR InterPro; IPR005323; CBM41_pullulanase.
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; 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; PF02806; Alpha-amylase_C; 1.
DR Pfam; PF02922; CBM_48; 1.
DR Pfam; PF03714; PUD; 2.
DR Pfam; PF21653; pulA_all-beta; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SMART; SM01066; CBM_25; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 2.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Glycosidase {ECO:0000313|EMBL:EFE90257.1};
KW Hydrolase {ECO:0000313|EMBL:EFE90257.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000003191};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..1708
FT /note="1,4-alpha-D-glucan glucanohydrolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009952178"
FT TRANSMEM 1670..1690
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 52..413
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 422..502
FT /note="Alpha-amylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00632"
FT DOMAIN 531..608
FT /note="Carbohydrate binding module family 25"
FT /evidence="ECO:0000259|SMART:SM01066"
FT REGION 506..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1593..1654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1595..1614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1615..1654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1708 AA; 182183 MW; D613A137478D1021 CRC64;
MAVRRFSSLA KRLAVTGIAV AMSATTLVAL PASADEAEAN AQARTSVGAP GDVIAIAFQT
NWNSVAKECT EAYGPEGVGY VQVSPPMESI QGTEWWTSYQ PVSYKLDSKL GTEAEFKTMI
ATCNAAGVEI IADSVINHTT GADQGEGTGV AGSKYDGEGN FPAIPYAKEN FHDCTKNIGD
YTNADEVQNC RLTSLQDLDT SQEYVQDKLA DYMNRLLDLG VYGFRVDAVK HIATADVAAI
KAKLAEKSGR NADDIFFEQE VIGNASEAAE IQPSNYVANG KVSEFNFTNH LSVAFAGDIT
DASKGLAKVG GDGWVSSDKA AVWVTNWDTE RGSAITYKKG SKYLLANAFM LAYDYGQPHI
YSGYYFDNSD DGAPGATETS VPDMECPTDG SMTSGTWQCA ERWTAIRGMI GFHNAVNGTD
VTNWKAYDTN VLGFGRGDVG YLALNNSADD SKQTFQTSLP AGEYCNVYAT GDCSATVTVK
DDGTFDATLA KNSAIAIYAG ATKDSWTGTT KSDPSDPDLS VNDETKKAAA DTSRTIYYKL
PDGWKQAYLH YGIDGWAEQG HELMADAGNG WVKFTVDPKG KSFEYVFTDG GDNWDNPNGG
GNYTAQGHWT AVADHEASAG VPSDVQSYQP KTKVIVHYKP AEGDAVADRG VYMWGTDKNG
ATLNGAWHAF TGEDSYGKVF ETTIDGAYDA AKIGVIVTTE GWDKVGGDRT IDGSTGTAEI
WVDGANPDET LTEAPDGYKK AANQIDVTIH YHRLADDYTS EDGMKAWDIW GWADGVNGAA
YPFTEHDDYG LIAKYTLKGS GMSTPQFIVR YGGDSWEAKD PNDENRTIPQ SAITVNADGT
ASAEIWLVQG DTTIYTNGTL YDAKGMIVSA EMTDFNTITV KLNKALTIDK PADAVSVEGV
KIKDVKASGN TVTITTSDNL DVTKAYKVTI EDYGAQNVSL GAVVRSDAFD KKYAYDGDDL
GVTYKAEKST FKLWAPTATK VTLRLYADST DPKAAQTDAV TLEKSGKKGV WTFAVDKDLK
DYAYDYELTF ADGTVNTSAD PYATAAVANG ERSVVLSGKE KGDAGKRMAS FSKPTDAIIT
EANVRDMTIN PNSGVSEANR GKYLGFVEEG TTVDGKQGAA STGIDYLKSL GVTHVQIMPV
YDYGSVDETG DLSYGAQYNW GYDPENYNVP EGSYSSDPSD PSARVKEMKQ MVSGLHKNGL
YVVMDVVYNH VYNASEHAFN KTVPGYYFRY DANGNLTNGS GCGNDVASER AMARKYIVDS
VKYWATEYNV DGFRFDLMGL IDQTTMNQVR AALDEIDPSI LVIGEGWDMT DAIGNQETTQ
PNASKVKGVA FFNDSLRDAI KGSVFSDEDT GFIAGKADKE NLIATNVLGC NNKREGIDEN
GHCNNGTADT NYGGADQVVQ YVEIHDNLTL YDKLVKSAPN DSEETRLARA KLADSLILLS
QGIADMQFGQ EFLRTKGGNG NSYNAGDAVN AIDWNRTVEQ AGSVNYVKGL IALRKSIKNL
HLSSYDDIAK NMTVLQQSDG VVAYQLKDGG DTYVVVFNAN ESAATVEAVP AGKYTVLAAD
GKVTETQDKN AATTVGADGY QAGALAAAVL KAGADDDSTK PDGGKDDSSK PGNNDGKDDN
QSGGTATPGT PGDSGNGNGQ TGDGNASNGA SDTAAGQSQQ FGAAALPNTG VALSVMAVAV
LVMTAAGMLL QRFSKGGNVV NSKEGSEQ
//
