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CDGT_BACLI
ID   CDGT_BACLI              Reviewed;         718 AA.
AC   P14014;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Cyclomaltodextrin glucanotransferase;
DE            EC=2.4.1.19;
DE   AltName: Full=Cyclodextrin-glycosyltransferase;
DE            Short=CGTase;
DE   Flags: Precursor;
GN   Name=cgtA;
OS   Bacillus licheniformis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2137908; DOI=10.1093/nar/18.1.199;
RA   Hill D.E., Aldape R., Rozzell J.D.;
RT   "Nucleotide sequence of a cyclodextrin glucosyltransferase gene, cgtA, from
RT   Bacillus licheniformis.";
RL   Nucleic Acids Res. 18:199-199(1990).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cyclizes part of a (1->4)-alpha-D-glucan chain by formation of
CC         a (1->4)-alpha-D-glucosidic bond.; EC=2.4.1.19;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 2 calcium ions per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- DOMAIN: May consist of two protein domains: the one in the N-terminal
CC       side cleaves the alpha-1,4-glucosidic bond in starch, and the other in
CC       the C-terminal side catalyzes other activities, including the
CC       reconstitution of an alpha-1,4-glucosidic linkage for cyclizing the
CC       maltooligosaccharide produced.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; X15752; CAA33763.1; -; Genomic_DNA.
DR   PIR; S15920; ALBSMX.
DR   AlphaFoldDB; P14014; -.
DR   SMR; P14014; -.
DR   CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   BRENDA; 2.4.1.19; 669.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:InterPro.
DR   GO; GO:0043895; F:cyclomaltodextrin glucanotransferase 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.10; -; 2.
DR   Gene3D; 2.60.40.1180; -; 1.
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; IPR002044; CBM_fam20.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
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; IPR002909; IPT_dom.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02806; Alpha-amylase_C; 1.
DR   Pfam; PF00686; CBM_20; 1.
DR   Pfam; PF01833; TIG; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SMART; SM01065; CBM_2; 1.
DR   SUPFAM; SSF49452; SSF49452; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   PROSITE; PS51166; CBM20; 1.
PE   3: Inferred from homology;
KW   Calcium; Disulfide bond; Glycosyltransferase; Metal-binding; Secreted;
KW   Signal; Transferase.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000250"
FT   CHAIN           35..718
FT                   /note="Cyclomaltodextrin glucanotransferase"
FT                   /id="PRO_0000001432"
FT   DOMAIN          532..612
FT                   /note="IPT/TIG"
FT   DOMAIN          613..718
FT                   /note="CBM20"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT   REGION          35..172
FT                   /note="A1"
FT   REGION          173..236
FT                   /note="B"
FT   REGION          237..440
FT                   /note="A2"
FT   REGION          441..528
FT                   /note="C"
FT   REGION          529..614
FT                   /note="D"
FT   REGION          615..718
FT                   /note="E"
FT   ACT_SITE        263
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        291
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         61
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         63
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         66
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         67
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         87
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         134..135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         224
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         227..230
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         233
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         266..267
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         267
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         361
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         405
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         409
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            362
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   DISULFID        77..84
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   718 AA;  78003 MW;  B3CDE14A81D5DC4E CRC64;
     MFQMAKRVLL STTLTFSLLA GSALPFLPAS AIYADADTAV TNKQNFSTDV IYQVFTDRFL
     DGNPSNNPTG AAFDGTCSNL KLYCGGDWQG LVNKINDNYF SDLGVTALWI SQPVENIFAT
     INYSGVTNTA YHGYWARDFK KTNPYFGTMT DFQNLVTTAH AKGIKIIIDF APNHTSPAME
     TDTSFAENGK LYDNGNLVGG YTNDTNGYFH HNGGSDFSTL ENGIYKNLYD LADLNHNNST
     IDTYFKDAIK LWLDMGVDGI RVDAVKHMPQ GWQKNWMSSI YAHKPVFTFG EWFLGSAAPD
     ADNTDFANES GMSLLDFRFN SAVRNVFRDN TSNMYALDSM LTATAADYNQ VNDQVTFIDN
     HDMDRFKTSA VNNRRLEQAL AFTLTSRGVP AIYYGTEQYL TGNGDPDNRG KMPSFSKSTT
     AFNVISKLAP LRKSNPAIAY GSTQQRWINN DVYIYERKFG KSVAVVAVNR NLTTPTSITN
     LNTSLPSGTY TDVLGGVLNG NNITSSGGNI SSFTLAAGAT AVWQYTASET TPTIGHVGPV
     MGKPGNVVTI DGRGFGSAKG TVYFGTTAVT GSAITSWEDT QIKVTIPPVA GGDYAVKVAA
     NGVNSNAYND FTILSGDQVS VRFVINNATT ALGENIYLTG NVSELGNWTT GAASIGPAFN
     QVIHAYPTWY YDVSVPAGKQ LEFKFFKKNG ATITWEGGSN HTFTTPTSGT ATVTINWQ
 
 
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