ID   CTA2_NIACI              Reviewed;         964 AA.
AC   P70873;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Cycloisomaltooligosaccharide glucanotransferase;
DE            Short=CITase;
DE            EC=2.4.1.248;
DE   Flags: Precursor;
GN   Name=cit;
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=U-155;
RA   Oguma T., Kurokawa T., Tobe K., Kitao S., Kobayashi M.;
RT   "Purification and some properties of cycloisomaltooligosaccharide
RT   glucanotransferase and cloning of cit gene from Bacillus circulans U-155.";
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Produces cycloisomaltooligosaccharide from dextran.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cyclizes part of a (1->6)-alpha-D-glucan chain by formation of
CC         a (1->6)-alpha-D-glucosidic bond.; EC=2.4.1.248;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 66 family. {ECO:0000305}.
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DR   EMBL; D88360; BAA13595.1; -; Genomic_DNA.
DR   AlphaFoldDB; P70873; -.
DR   SMR; P70873; -.
DR   CAZy; CBM35; Carbohydrate-Binding Module Family 35.
DR   CAZy; GH66; Glycoside Hydrolase Family 66.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd14745; GH66; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   InterPro; IPR011635; CARDB.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR025092; Glyco_hydro_66.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF07705; CARDB; 1.
DR   Pfam; PF16990; CBM_35; 1.
DR   Pfam; PF03422; CBM_6; 1.
DR   Pfam; PF13199; Glyco_hydro_66; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   PROSITE; PS51175; CBM6; 2.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Repeat; Signal; Transferase.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..964
FT                   /note="Cycloisomaltooligosaccharide glucanotransferase"
FT                   /id="PRO_0000012242"
FT   DOMAIN          413..538
FT                   /note="CBM6 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00523"
FT   DOMAIN          740..863
FT                   /note="CBM6 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00523"
SQ   SEQUENCE   964 AA;  107208 MW;  8849CDC5E2DE9A68 CRC64;
     MRVKILPLVF MTLLLIVPSQ MLLPSGQANA STPGFIERVY TDKARYEPGE LVTVTAQINN
     SGGTNWSGDV TMTIFHLENA VYSSVQHASI ASGQTTDVTF SWTSDTTDFK GYFVSVDAGS
     LGQGYSSIDV SSDFAKYPRY GYISEFSSNE TAAESAAKVN ELAQDYKINA WQFYDWMWRH
     ETMIKRTGGT IDPTWIDLFN RQISWPTINN QIAAIHNQNG AAMAYAMIYA ARENYSGFGV
     NPEWGMYMDP AHTKQLDVDF GNNSTYMYLF DPANAGWQQF IHEQYLDAIQ TANFDGIHID
     QMGQRNNIYD YSGNSIDLAT RFTPFIKAAK TKLTAANSNQ DFMTFNIVDG TVNGWAANDV
     SKNANVDFLY SEIWHLSNSY MQLKDYIDSL RANSGNKAVV LAAYMNYGEN IGDRYEAEDA
     ALQHTAVNTD HAGYTGSGFV DQFADVNDSV TFTITAPEEG YYSLVFRFAN HSGYTATRNL
     YVDSNFEIEL PFQNQPNWDT WSHETWHQVY LTPGTHTIKL SYDSSNTGAI NLDSLTLGTF
     DEHSIRLADA MMAASGATHI ELGEDSQMLA HEYYPNRSKS MRSTLKSAMK DHYNFITAYE
     NLLFDADVID NDAGKQFINI AGVNTSPDGA ANTVWHMSKR TPEYNILHLI NLVNNDQNWR
     NSGNQPTAQT NLATKVYIGA EETITGVYAA SPDHNQGATQ SLPFTTGTDS SGSYISFTVP
     SLEYWSMIYM KRSTAAPVDN MYEAETAIKS NVSVNTNHAG YTGSGFVDQF ATVNDGVSFI
     VHASSKDDYV LRFRYSNGGS DANRDVFLNG KYAGTVQLKH TGGWNQWAYG ELTVPLAQGS
     HSVVLWYNSS NSGAVNLDHL KLDKTYIWQF DRQIASVPAG YRITFKAGLP GWVHFGTDNW
     KNVMDIPLAS NGSSDSSLNY EASIGPFPSA TTVDVTFLWD DNNNGILEDM IDRWEGTDFQ
     IAIP