ID CDGT_KLEOX STANDARD; PRT; 655 AA. AC P08704; DT 01-JAN-1988 (Rel. 06, Created) DT 01-JAN-1988 (Rel. 06, Last sequence update) DT 01-FEB-2005 (Rel. 46, Last annotation update) DE Cyclomaltodextrin glucanotransferase precursor (EC 2.4.1.19) DE (Cyclodextrin-glycosyltransferase) (CGTase). GN Name=cgt; OS Klebsiella oxytoca. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=571; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M5a1; RX MEDLINE=87163498; PubMed=2951300; DOI=10.1016/0378-1119(86)90070-3; RA Binder F., Huber O., Boeck A.; RT "Cyclodextrin-glycosyltransferase from Klebsiella pneumoniae M5a1: RT cloning, nucleotide sequence and expression."; RL Gene 47:269-277(1986). CC -!- CATALYTIC ACTIVITY: Cyclizes part of a 1,4-alpha-D-glucan chain by CC formation of a 1,4-alpha-D-glucosidic bond. CC -!- COFACTOR: Binds 2 calcium ions per subunit (By similarity). CC -!- SUBUNIT: Monomer. CC -!- DOMAIN: May consist of two protein domains: the one in the N- CC terminal side cleaves the alpha-1,4-glucosidic bond in starch, and CC the other in the C-terminal side catalyzes other activities, CC including the reconstitution of an alpha-1,4-glucosidic linkage CC for cyclizing the maltooligosaccharide produced. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. CC -------------------------------------------------------------------------- CC This Swiss-Prot entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use as long as its content is in no way modified and this statement is not CC removed. CC -------------------------------------------------------------------------- DR EMBL; M15264; AAA25059.1; -. DR PIR; A29023; ALKBG. DR HSSP; P19531; 1QHP. DR InterPro; IPR006589; Alp_amyl_cat_sub. DR InterPro; IPR006048; Alpha_amyl_C. DR InterPro; IPR006047; Alpha_amyl_cat. DR InterPro; IPR002044; Glyco_hydro_CBD. DR Pfam; PF00128; Alpha-amylase; 1. DR Pfam; PF02806; Alpha-amylase_C; 1. DR Pfam; PF00686; CBM_20; 1. DR ProDom; PD001568; Glyco_hydro_CBD; 1. DR SMART; SM00642; Aamy; 1. DR SMART; SM00632; Aamy_C; 1. KW Calcium-binding; Glycosyltransferase; Signal; Transferase. FT SIGNAL 1 30 FT CHAIN 31 655 Cyclomaltodextrin glucanotransferase. FT ACT_SITE 253 253 Nucleophile (By similarity). FT ACT_SITE 287 287 Proton donor (By similarity). FT ACT_SITE 363 363 By similarity. FT METAL 55 55 Calcium 2 (By similarity). FT METAL 60 60 Calcium 2 (By similarity). FT METAL 61 61 Calcium 2 (By similarity). FT METAL 79 79 Calcium 2 (via carbonyl oxygen) (By FT similarity). FT METAL 81 81 Calcium 2 (By similarity). FT METAL 164 164 Calcium 1 (By similarity). FT METAL 223 223 Calcium 1 (By similarity). FT METAL 257 257 Calcium 1 (via carbonyl oxygen) (By FT similarity). SQ SEQUENCE 655 AA; 73025 MW; DB8F26332BED26A7 CRC64; MKRNRFFNTS AAIAISIALN TFFCSMQTIA AEPEETYLDF RKETIYFLFL DRFSDGDPSN NAGFNSATYD PNNLKKYTGG DLRGLINKLP YLKSLGVTSI WITPPIDNVN NTDAAGNTGY HGYWGRDYFR IDEHFGNLDD FKELTSLMHS PDYNMKLVLD YAPNHSNAND ENEFGALYRD GVFITDYPTN VAANTGWYHH NGGVTNWNDF FQVKNHNLFN LSDLNQSNTD VYQYLLDGSK FWIDAGVDAI RIDAIKHMDK SFIQKWTSDI YDYSKSIGRE GFFFFGEWFG ASANTTTGVD GNAIDYANTS GSALLDFGFR DTLERVLVGR SGNTMKTLNS YLIKRQTVFT SDDWQVVFMD NHDMARIGTA LRSNATTFGP GNNETGGSQS EAFAQKRIDL GLVATMTVRG IPAIYYGTEH YAANFTSNSF GQVGSDPYNR EKMPGFDTES EAFSIIKTLG DLRKSSPAIQ NGTYTELWVN DDILVFERRS GNDIVIVALN RGEANTINVK NIAVPNGVYP SLIGNNSVSV ANKRTTLTLM QNEAVVIRSQ SDDAENPTVQ SINFTCNNGY TISGQSVYII GNIPQLGGWD LTKAVKISPT QYPQWSASLE LPSDLNVEWK CVKRNETNPT ANVEWQSGAN NQFNSNDTQT TNGSF //