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CDGT1_NIACI
ID   CDGT1_NIACI             Reviewed;         718 AA.
AC   P30920;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Cyclomaltodextrin glucanotransferase;
DE            EC=2.4.1.19;
DE   AltName: Full=Cyclodextrin-glycosyltransferase;
DE            Short=CGTase;
DE   Flags: Precursor;
OS   Niallia circulans (Bacillus circulans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Niallia.
OX   NCBI_TaxID=1397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=8;
RX   PubMed=1368573; DOI=10.1007/bf00172548;
RA   Nitschke L., Heeger K., Bender H., Schulz G.E.;
RT   "Molecular cloning, nucleotide sequence and expression in Escherichia coli
RT   of the beta-cyclodextrin glycosyltransferase gene from Bacillus circulans
RT   strain no. 8.";
RL   Appl. Microbiol. Biotechnol. 33:542-546(1990).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RC   STRAIN=8;
RX   PubMed=1826034; DOI=10.1016/0022-2836(91)90530-j;
RA   Klein C., Schulz G.E.;
RT   "Structure of cyclodextrin glycosyltransferase refined at 2.0-A
RT   resolution.";
RL   J. Mol. Biol. 217:737-750(1991).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS).
RC   STRAIN=8;
RX   PubMed=2531228; DOI=10.1016/0022-2836(89)90607-4;
RA   Hofmann B.E., Bender H., Schulz G.E.;
RT   "Three-dimensional structure of cyclodextrin glycosyltransferase from
RT   Bacillus circulans at 3.4-A resolution.";
RL   J. Mol. Biol. 209:793-800(1989).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RC   STRAIN=8;
RX   PubMed=9558324; DOI=10.1021/bi9729918;
RA   Schmidt A.K., Cottaz S., Driguez H., Schulz G.E.;
RT   "Structure of cyclodextrin glycosyltransferase complexed with a derivative
RT   of its main product beta-cyclodextrin.";
RL   Biochemistry 37:5909-5915(1998).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RC   STRAIN=8;
RX   PubMed=9738912; DOI=10.1046/j.1432-1327.1998.2550710.x;
RA   Parsiegla G., Schmidt A.K., Schulz G.E.;
RT   "Substrate binding to a cyclodextrin glycosyltransferase and mutations
RT   increasing the gamma-cyclodextrin production.";
RL   Eur. J. Biochem. 255:710-717(1998).
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;
CC       Note=Binds 2 calcium ions per subunit.;
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; X68326; CAA48401.1; -; Genomic_DNA.
DR   PIR; S23674; ALBSGC.
DR   PDB; 1CGT; X-ray; 2.00 A; A=35-718.
DR   PDB; 1CGU; X-ray; 2.50 A; A=35-718.
DR   PDB; 3CGT; X-ray; 2.40 A; A=35-718.
DR   PDB; 4CGT; X-ray; 2.60 A; A=35-718.
DR   PDB; 5CGT; X-ray; 2.50 A; A=35-718.
DR   PDB; 6CGT; X-ray; 2.60 A; A=35-718.
DR   PDB; 7CGT; X-ray; 3.00 A; A=35-718.
DR   PDB; 8CGT; X-ray; 2.40 A; A=35-718.
DR   PDB; 9CGT; X-ray; 2.50 A; A=35-718.
DR   PDBsum; 1CGT; -.
DR   PDBsum; 1CGU; -.
DR   PDBsum; 3CGT; -.
DR   PDBsum; 4CGT; -.
DR   PDBsum; 5CGT; -.
DR   PDBsum; 6CGT; -.
DR   PDBsum; 7CGT; -.
DR   PDBsum; 8CGT; -.
DR   PDBsum; 9CGT; -.
DR   AlphaFoldDB; P30920; -.
DR   SMR; P30920; -.
DR   DrugBank; DB01789; 1-Amino-2,3-Dihydroxy-5-Hydroxymethyl Cyclohex-5-Ene.
DR   DrugBank; DB02469; 4,6-dideoxy-4-amino-beta-D-glucopyranoside.
DR   DrugBank; DB01841; 4,6-Dideoxyglucose.
DR   DrugBank; DB02670; 4-Deoxy-Alpha-D-Glucose.
DR   DrugBank; DB02120; 6-Amino-4-Hydroxymethyl-Cyclohex-4-Ene-1,2,3-Triol.
DR   DrugBank; DB01909; Alpha-Cyclodextrin (Cyclohexa-Amylose).
DR   DrugBank; DB03773; alpha-D-quinovopyranose.
DR   DrugBank; DB02379; Beta-D-Glucose.
DR   DrugBank; DB03323; Maltose.
DR   DrugBank; DB02394; Oxiranpseudoglucose.
DR   DrugBank; DB03198; Thio-Maltohexaose.
DR   DrugBank; DB01719; Thio-Maltopentaose.
DR   CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PRIDE; P30920; -.
DR   BRENDA; 2.4.1.19; 649.
DR   EvolutionaryTrace; P30920; -.
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   InterPro; IPR006311; TAT_signal.
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.
DR   PROSITE; PS51318; TAT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Disulfide bond; Glycosyltransferase; Metal-binding;
KW   Secreted; Signal; Transferase.
FT   SIGNAL          1..34
FT   CHAIN           35..718
FT                   /note="Cyclomaltodextrin glucanotransferase"
FT                   /id="PRO_0000001430"
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   BINDING         63
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT   BINDING         66
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT   BINDING         67
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT   BINDING         85
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT   BINDING         87
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT   BINDING         134..135
FT                   /ligand="substrate"
FT   BINDING         173
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT   BINDING         174
FT                   /ligand="substrate"
FT   BINDING         224
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT   BINDING         227..230
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         230
FT                   /ligand="substrate"
FT   BINDING         233
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT   BINDING         261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         266..267
FT                   /ligand="substrate"
FT   BINDING         267
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT   BINDING         267
FT                   /ligand="substrate"
FT   BINDING         361
FT                   /ligand="substrate"
FT   BINDING         405
FT                   /ligand="substrate"
FT   BINDING         409
FT                   /ligand="substrate"
FT   SITE            362
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   DISULFID        77..84
FT   STRAND          37..39
FT                   /evidence="ECO:0007829|PDB:1CGU"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   HELIX           56..59
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   HELIX           64..66
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   HELIX           70..72
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   HELIX           88..96
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   HELIX           99..103
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          107..110
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          114..116
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          121..123
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          126..128
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          135..142
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   TURN            144..146
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   HELIX           149..161
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          165..170
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          174..177
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   TURN            186..189
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          191..193
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          196..199
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          201..203
FT                   /evidence="ECO:0007829|PDB:4CGT"
FT   STRAND          217..219
FT                   /evidence="ECO:0007829|PDB:3CGT"
FT   HELIX           220..225
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          226..228
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          231..234
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   HELIX           239..254
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          259..263
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   HELIX           265..267
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   HELIX           270..283
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          287..290
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          295..298
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   HELIX           301..309
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          310..315
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   HELIX           317..327
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   HELIX           334..347
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   HELIX           351..353
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          354..356
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          369..371
FT                   /evidence="ECO:0007829|PDB:5CGT"
FT   HELIX           373..385
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          386..393
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   HELIX           396..398
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   HELIX           407..409
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   HELIX           420..428
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   HELIX           431..434
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   HELIX           436..440
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          442..448
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          450..459
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          462..469
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          476..478
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          487..490
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   TURN            493..498
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          503..506
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          513..515
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          520..525
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          533..538
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          540..542
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          547..553
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          561..564
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          567..569
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   HELIX           571..573
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          574..577
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          579..585
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          591..600
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          608..613
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          615..626
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          635..642
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   HELIX           643..645
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   TURN            646..648
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          651..655
FT                   /evidence="ECO:0007829|PDB:6CGT"
FT   STRAND          661..664
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          669..676
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          680..691
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          693..695
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          701..704
FT                   /evidence="ECO:0007829|PDB:1CGT"
FT   STRAND          707..716
FT                   /evidence="ECO:0007829|PDB:1CGT"
SQ   SEQUENCE   718 AA;  78047 MW;  E08CF0FE9C98BDA1 CRC64;
     MFQMAKRAFL STTLTLGLLA GSALPFLPAS AVYADPDTAV TNKQSFSTDV IYQVFTDRFL
     DGNPSNNPTG AAYDATCSNL KLYCGGDWQG LINKINDNYF SDLGVTALWI SQPVENIFAT
     INYSGVTNTA YHGYWARDFK KTNPYFGTMA DFQNLITTAH AKGIKIVIDF APNHTSPAME
     TDTSFAENGR LYDNGTLVGG YTNDTNGYFH HNGGSDFSSL ENGIYKNLYD LADFNHNNAT
     IDKYFKDAIK LWLDMGVDGI RVDAVKHMPL GWQKSWMSSI YAHKPVFTFG EWFLGSAASD
     ADNTDFANKS GMSLLDFRFN SAVRNVFRDN TSNMYALDSM INSTATDYNQ VNDQVTFIDN
     HDMDRFKTSA VNNRRLEQAL AFTLTSRGVP AIYYGTEQYL TGNGDPDNRA KMPSFSKSTT
     AFNVISKLAP LRKSNPAIAY GSTQQRWINN DVYVYERKFG KSVAVVAVNR NLSTSASITG
     LSTSLPTGSY TDVLGGVLNG NNITSTNGSI NNFTLAAGAT AVWQYTTAET TPTIGHVGPV
     MGKPGNVVTI DGRGFGSTKG TVYFGTTAVT GAAITSWEDT QIKVTIPSVA AGNYAVKVAA
     SGVNSNAYNN FTILTGDQVT VRFVVNNAST TLGQNLYLTG NVAELGNWST GSTAIGPAFN
     QVIHQYPTWY YDVSVPAGKQ LEFKFFKKNG STITWESGSN HTFTTPASGT ATVTVNWQ
 
 
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