ID   MALQ_CLOBU              Reviewed;         487 AA.
AC   Q59266;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=4-alpha-glucanotransferase;
DE            EC=2.4.1.25;
DE   AltName: Full=Amylomaltase;
DE   AltName: Full=Disproportionating enzyme;
DE            Short=D-enzyme;
GN   Name=malQ;
OS   Clostridium butyricum.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1492;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=ATCC 19398 / DSM 10702 / JCM 1391 / NCIMB 7423;
RX   PubMed=9353929; DOI=10.1099/00221287-143-10-3287;
RA   Goda S.K., Eissa O., Akhtar M., Minton N.P.;
RT   "Molecular analysis of a Clostridium butyricum NCIMB 7423 gene encoding 4-
RT   alpha-glucanotransferase and characterization of the recombinant enzyme
RT   produced in Escherichia coli.";
RL   Microbiology 143:3287-3294(1997).
CC   -!- FUNCTION: Catalyzes a disproportionation reaction in which single or
CC       multiple glucose units from oligosaccharides are transferred to the 4-
CC       hydroxyl group of acceptor sugars. Glucose, maltose and maltotriose can
CC       act as acceptor, whereas of the three only maltotriose can act as
CC       donor.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Transfers a segment of a (1->4)-alpha-D-glucan to a new
CC         position in an acceptor, which may be glucose or a (1->4)-alpha-D-
CC         glucan.; EC=2.4.1.25;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the disproportionating enzyme family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L37874; AAB84229.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q59266; -.
DR   SMR; Q59266; -.
DR   CAZy; GH77; Glycoside Hydrolase Family 77.
DR   PRIDE; Q59266; -.
DR   BRENDA; 2.4.1.25; 1465.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004134; F:4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102500; F:beta-maltose 4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016757; F:glycosyltransferase activity; IDA:CACAO.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR003385; Glyco_hydro_77.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR32438; PTHR32438; 1.
DR   Pfam; PF02446; Glyco_hydro_77; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   TIGRFAMs; TIGR00217; malQ; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cytoplasm; Glycosyltransferase; Transferase.
FT   CHAIN           1..487
FT                   /note="4-alpha-glucanotransferase"
FT                   /id="PRO_0000170124"
SQ   SEQUENCE   487 AA;  57178 MW;  FA9FBE3E74771DBE CRC64;
     MHISSLPGKY GIGTFGRSAY EFCDFLEKAG QKYWQILPLG QTSYGDSPYQ SFSAFAGNPY
     FIDLDILNEK NLLDKDDYEE KNFGDNKEMI NYGLIFNEKM KVLRKAYMNF NSKDDESFAK
     FIEDEKKWLD DYSLFMALKY KFNFISWNSW NKDIKLRKNE EIEKYKDELK EDVNYWKFLQ
     YEFFSQWKNL KDYANKKNIK IIGDIPIYIA QDSSDVWSNP DIFLLNKETL EPLKVSGCPP
     DAFSETGQLW GNPIYDWGYL EKTNFEWWVD RIKSSLKLYD ILRIDHFRGF EAYWSVDYGE
     KTAQNGKWIK GPEMKLFNVI KEKIGDIEII AEDLGYLTEE TLEFKKRTGF PGMKIIQFAF
     GGDSSNPYLP HNYEKNCVAY TGTHDNDTVR GWFEVTGSKE EKEKAVEYFK LTEEEGYNWG
     VIRGVWSSVA NTSIGVMQDF LNLGNEARIN KPSTLASNWS WRAKDNVFTN ELANKIYRLT
     RIYGRCE