AMYB_THETU
ID AMYB_THETU Reviewed; 551 AA.
AC P19584;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Thermophilic beta-amylase;
DE EC=3.2.1.2;
DE AltName: Full=1,4-alpha-D-glucan maltohydrolase;
DE Flags: Precursor;
OS Thermoanaerobacterium thermosulfurigenes (Clostridium thermosulfurogenes).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family III. Incertae Sedis; Thermoanaerobacterium.
OX NCBI_TaxID=33950;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 33-44.
RC STRAIN=ATCC 33743 / DSM 2229 / 4B;
RX PubMed=2461360; DOI=10.1128/jb.170.12.5848-5854.1988;
RA Kitamoto N., Yamagata H., Kato T., Tsukagoshi N., Udaka S.;
RT "Cloning and sequencing of the gene encoding thermophilic beta-amylase of
RT Clostridium thermosulfurogenes.";
RL J. Bacteriol. 170:5848-5854(1988).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides so as to remove successive maltose units from the
CC non-reducing ends of the chains.; EC=3.2.1.2;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P36924};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P36924};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 75 degrees Celsius. Stable at 80 degrees
CC Celsius.;
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 14 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M22471; AAA23204.1; -; Genomic_DNA.
DR PIR; A31389; A31389.
DR AlphaFoldDB; P19584; -.
DR SMR; P19584; -.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR CAZy; GH14; Glycoside Hydrolase Family 14.
DR GO; GO:0102229; F:amylopectin maltohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016161; F:beta-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd05809; CBM20_beta_amylase; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR034835; CBM20_beta_amylase.
DR InterPro; IPR002044; CBM_fam20.
DR InterPro; IPR001554; Glyco_hydro_14.
DR InterPro; IPR018238; Glyco_hydro_14_CS.
DR InterPro; IPR000125; Glyco_hydro_14A_bac.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR31352; PTHR31352; 1.
DR Pfam; PF00686; CBM_20; 1.
DR Pfam; PF01373; Glyco_hydro_14; 1.
DR PRINTS; PR00750; BETAAMYLASE.
DR PRINTS; PR00841; GLHYDLASE14A.
DR SMART; SM01065; CBM_2; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00506; BETA_AMYLASE_1; 1.
DR PROSITE; PS00679; BETA_AMYLASE_2; 1.
DR PROSITE; PS51166; CBM20; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Direct protein sequencing; Glycosidase; Hydrolase;
KW Metal-binding; Polysaccharide degradation; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000269|PubMed:2461360"
FT CHAIN 33..551
FT /note="Thermophilic beta-amylase"
FT /id="PRO_0000001456"
FT DOMAIN 448..551
FT /note="CBM20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT ACT_SITE 195
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10050"
FT ACT_SITE 392
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P36924"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36924"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P36924"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36924"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36924"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P36924"
FT BINDING 310
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36924"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36924"
FT BINDING 353
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36924"
FT BINDING 393..394
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36924"
FT BINDING 423
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36924"
SQ SEQUENCE 551 AA; 60548 MW; 58526A1067275AC2 CRC64;
MIGAFKRLGQ KLFLTLLTAS LIFASSIVTA NASIAPNFKV FVMGPLEKVT DFNAFKDQLI
TLKNNGVYGI TTDIWWGYVE NAGENQFDWS YYKTYADTVR AAGLKWVPIM STHACGGNVG
DTVNIPIPSW VWTKDTQDNM QYKDEAGNWD NEAVSPWYSG LTQLYNEFYS SFASNFSSYK
DIITKIYISG GPSGELRYPS YNPSHGWTYP GRGSLQCYSK AAITSFQNAM KSKYGTIAAV
NSAWGTSLTD FSQISPPTDG DNFFTNGYKT TYGNDFLTWY QSVLTNELAN IASVAHSCFD
PVFNVPIGAK IAGVHWLYNS PTMPHAAEYC AGYYNYSTLL DQFKASNLAM TFTCLEMDDS
NAYVSPYYSA PMTLVHYVAN LANNKGIVHN GENALAISNN NQAYVNCANE LTGYNFSGFT
LLRLSNIVNS DGSVTSEMAP FVINIVTLTP NGTIPVTFTI NNATTYYGQN VYIVGSTSDL
GNWNTTYARG PASCPNYPTW TITLNLLPGE QIQFKAVKID SSGNVTWEGG SNHTYTVPTS
GTGSVTITWQ N
