ID A0A0D6ZGX1_9BACI Unreviewed; 2277 AA.
AC A0A0D6ZGX1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Amylopullulanase {ECO:0000313|EMBL:KIY23893.1};
GN ORFNames=UB32_00425 {ECO:0000313|EMBL:KIY23893.1};
OS Mesobacillus subterraneus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX NCBI_TaxID=285983 {ECO:0000313|EMBL:KIY23893.1, ECO:0000313|Proteomes:UP000032512};
RN [1] {ECO:0000313|EMBL:KIY23893.1, ECO:0000313|Proteomes:UP000032512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MITOT1 {ECO:0000313|EMBL:KIY23893.1,
RC ECO:0000313|Proteomes:UP000032512};
RA Peet K.C., Thompson J.R.;
RT "Draft genome sequences of the supercritical CO2 tolerant bacteria Bacillus
RT subterraneus MITOT1 and Bacillus cereus MIT0214.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KIY23893.1}.
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DR EMBL; JXIQ01000002; KIY23893.1; -; Genomic_DNA.
DR RefSeq; WP_044390279.1; NZ_JXIQ01000002.1.
DR SMR; A0A0D6ZGX1; -.
DR PATRIC; fig|285983.3.peg.2725; -.
DR OrthoDB; 9761875at2; -.
DR Proteomes; UP000032512; Unassembled WGS sequence.
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; 3.
DR CDD; cd02860; E_set_Pullulanase; 1.
DR Gene3D; 2.60.40.1110; -; 3.
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; 2.
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; IPR011838; Pullulan_Gpos.
DR InterPro; IPR001119; SLH_dom.
DR InterPro; IPR040806; SpuA_C.
DR NCBIfam; TIGR02102; pullulan_Gpos; 1.
DR PANTHER; PTHR43002; GLYCOGEN DEBRANCHING ENZYME; 1.
DR Pfam; PF00128; Alpha-amylase; 2.
DR Pfam; PF02922; CBM_48; 1.
DR Pfam; PF03714; PUD; 3.
DR Pfam; PF00395; SLH; 3.
DR Pfam; PF18033; SpuA_C; 1.
DR SMART; SM00642; Aamy; 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; 3.
DR PROSITE; PS51272; SLH; 3.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000032512};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..2277
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002316093"
FT DOMAIN 2083..2146
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 2147..2208
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 2216..2277
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT REGION 1846..1873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2277 AA; 250708 MW; DC02BEF930F80B68 CRC64;
MVMKKNTKRN FSIFMTAVMI LSLWLPFVPA PQAFAVDSSA AVEVTDRTVR VNYIREDQQY
DGWNIWVWNT GRQNDQINFQ SYENGMAAAD IAVAPETASI GLLIRSTDNW NTAVKEFDKD
RIIPVNKNDS ITKAFITSGV EQMRIVPDGS APVIDQGNAT FYYRDKTLFA NNTMDTIKKV
ELKFNGDIIP MIYEPENERF VATYEGIPNG TTPYTFAVTM EDGTTTEVQD PYNPTSDIVF
QKGELTVAGT VAPAAIDYNQ NAVLTVDVQG MTNEVTINKI TADISALGGS KQLEIDPALK
EVTIAVDDNI TAGIKEVPLT VVDSFGNLYN GTASVEIKTR QAVGENDFDW DESIIYFMLT
DRFFDGDSTN NDPYHQNYDT TDRGTYQGGD FKGITEKLDY LDDLGVNTIW ISPIVENIKH
DVRYQDGDPS YYAYHGYWAS NFGKLNPHFG TMDDFHNLID AAHERGIKIM VDVVLNHTGY
GLKDIDNQVT NPPAGYPTDE ERSVFSGLLR QGSNVGSDEV RGELAGLPDL KTEDPAVRKT
IIDWQTDWID KAKTAKGNTI DYFRVDTVKH VEDTTWMAFK NAITEKMPEH KMIGESWGAS
AQNDYGYLET GMMDSLLDFG FKNIAHDFVN GKLESANDAL IDRNGKIDNN ATLGQFLGSH
DEDGFLFKEG NDEGKLKLAA SLQATAKGQP VIYYGEELGQ SGANNYPQND NRYDLAWDQI
EGNAILDHYK KVLNFRDDYS EVFAKGERTT IGGTDAEKFI FFARKYGNEA AYVGLNIADT
AKKISLTVAP GSVITDHYSN QTFTASQAGE ITWTIPAKAD GGTVLLTVDG GEITAATSTE
DDGGNGTIVE PIPANHVRIH YKRNDNNYEN FGAWLWNDVA SPSANWPTGA TMFEKMDSYG
AYIDVELKDG AKNIGFLAMD ITKGDAGKDG GDKGFTVTSP EINEIFIKQG DDTVYKYEPV
DLPANTVRVH YVRDNADYEN FGLWFWGDVT SPPSNWTADA PSFENIDRYG AYVDIQLNEN
AKEIGMITLN KATQEKDGGD KKFNLLDKYN HVWVKQGDDN VYVSPYWEQA SGLVSAEVLN
ESTILLGFTL TDGLTPEALT DALEIKDADG TAVTIDSVEI TGTTSVKITA QFALDKLPLS
ITYAGRTVSA ASGWRMLDDM YAYDGNDLGA TYKDGGATLK LWAPKASQVV ANFFNKDNAN
EKIGSINLEK GNKGVWSVDV APGDLNITDL EGYFYQYDVT NDEVTRQVLD PYAKSLAAFT
VNTKGEAGPD GDTVGKAAIV DLSDTDPEGF DHAKIDGYEK REDAVIYEVH VRDFTSDPSI
EDDLNARWGS YKAFEDKLEY IKSLGVTHVQ LLPVMAWYYG DETKMAEREL DYAAGGNEYN
WGYDPHSYFS PDGAYSLDPT NPELRVKELK QMIDAIHDAG MGVVLDVVYT HMAKASQLND
IVPDYYAFKD AQGNFLGGFG NNLATSHTMA EKLMVDSVKY WFEEYKIDGM RFDMMGDATY
PSIQNAYDAA ADVNPDALFL GEGWRTFAGH IAEPELAGMG ADQDWMDKTD DVGVFSDEIR
NELKSGFGSE GEPRFITGGA RDINTIFNNI KGQPGNTADD DPGDMVQYIA AHDNLTLHDV
IVQSIKKDPA VPENELEIHK RIRLGNSIIL TSQGTAFLHA GQEYGRTKQW KGEGVPDQKY
HELKDEQGKS FGYFIHDSYD SSDAINMFDW QKATNKEEYA VNTTTKAFTQ GLIELRKSTN
AFRLGDMELV DQNVTLLNFP EIQNNDLVIA YENVSTDNTG NYYVFVNADS QPRSLTLGDY
NFSGGKVLVD SDEAGAKPVS EKSGFRLSRD TLTIDPLTTI VIKLDRRATD SPADNGDGNP
NPPAPPAGKP NTIELPAGAA EVVKEKNPSG MIDVITKVMA NKVAEVVHAI TADKTNIAVK
LENPATGEKA KAQLPISLFI EAAKKSQQAT VEIVTGNASY TLPVSEINVD DIAEKLGVSA
SDVQITVSVN VVKPDDKSKL NMKSAMIDFT VEAAASNKKT EIKKFSAYVE REILGDTSFN
TAKTVAVKLN EDGTFSSVPT LFDGNKAMIK SLTNSTYTIV ENDVTFTDVN NGMDWAEPYI
EALASKYIIK GKGDGTFGST QQLTRAEFTA LLVRALGLPG EQYDDRFKDV NGSEWFNDNN
ALMAAIEYGI IQGKGNGTFA PGEKITRTEA AAMIGRAMKL EFINYDLSTL DKTNTLRNFT
DAGSIGNWAK ADVESVYQAG IINGKATDKF GAAGSTQRNE MAKILANFLE KAKLLNY
//