CDGT2_PAEMA
ID CDGT2_PAEMA Reviewed; 713 AA.
AC P31835;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Cyclomaltodextrin glucanotransferase;
DE EC=2.4.1.19;
DE AltName: Full=Cyclodextrin-glycosyltransferase;
DE Short=CGTase;
DE Flags: Precursor;
OS Paenibacillus macerans (Bacillus macerans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=44252;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 28-37.
RA Sugimoto T., Kubota M., Sakai S.;
RT "Polypeptide possessing cyclomaltodextrin glucanotransferase activity.";
RL Patent number GB2169902, 23-JUL-1986.
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 PIR; S26589; ALBSXR.
DR AlphaFoldDB; P31835; -.
DR SMR; P31835; -.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR BRENDA; 2.4.1.19; 670.
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; 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; 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 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Glycosyltransferase; Metal-binding;
KW Secreted; Signal; Transferase.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|Ref.1"
FT CHAIN 28..713
FT /note="Cyclomaltodextrin glucanotransferase"
FT /id="PRO_0000001435"
FT DOMAIN 526..606
FT /note="IPT/TIG"
FT DOMAIN 608..713
FT /note="CBM20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT REGION 28..165
FT /note="A1"
FT REGION 166..229
FT /note="B"
FT REGION 230..434
FT /note="A2"
FT REGION 435..522
FT /note="C"
FT REGION 523..609
FT /note="D"
FT REGION 610..713
FT /note="E"
FT ACT_SITE 256
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 285
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 127..128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 220..223
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 259..260
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 355
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 399
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 403
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 356
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 713 AA; 76857 MW; 5A287BCC4AAFE635 CRC64;
MKKQVKWLTS VSMSVGIALG AALPVWASPD TSVNNKLNFS TDTVYQIVTD RFVDGNSANN
PTGAAFSSDH SNLKLYFGGD WQGITNKIND GYLTGMGITA LWISQPVENI TAVINYSGVN
NTAYHGYWPR DFKKTNAAFG SFTDFSNLIA AAHSHNIKVV MDFAPNHTNP ASSTDPSFAE
NGALYNNGTL LGKYSNDTAG LFHHNGGTDF STTESGIYKN LYDLADINQN NNTIDSYLKE
SIQLWLNLGV DGIRFDAVKH MPQGWQKSYV SSIYSSANPV FTFGEWFLGP DEMTQDNINF
ANQSGMHLLD FAFAQEIREV FRDKSETMTD LNSVISSTGS SYNYINNMVT FIDNHDMDRF
QQAGASTRPT EQALAVTLTS RGVPAIYYGT EQYMTGNGDP NNRGMMTGFD TNKTAYKVIK
ALAPLRKSNP ALAYGSTTQR WVNSDVYVYE RKFGSNVALV AVNRSSTTAY PISGALTALP
NGTYTDVLGG LLNGNSITVN GGTVSNFTLA AGGTAVWQYT TTESSPIIGN VGPTMGKPGN
TITIDGRGFG TTKNKVTFGT TAVTGANIVS WEDTEIKVKV PNVAAGNTAV TVTNAAGTTS
AAFNNFNVLT ADQVTVRFKV NNATTALGQN VYLTGNVAEL GNWTAANAIG PMYNQVEASY
PTWYFDVSVP ANTALQFKFI KVNGSTVTWE GGNNHTFTSP SSGVATVTVD WQN
