ID   MALQ_MYCTO              Reviewed;         724 AA.
AC   P9WK22; L0TAL4; O53932; P65336;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 39.
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; OrderedLocusNames=MT1831;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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}.
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DR   EMBL; AE000516; AAK46101.1; -; Genomic_DNA.
DR   PIR; G70928; G70928.
DR   RefSeq; WP_003408795.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WK22; -.
DR   SMR; P9WK22; -.
DR   CAZy; GH77; Glycoside Hydrolase Family 77.
DR   EnsemblBacteria; AAK46101; AAK46101; MT1831.
DR   GeneID; 45425759; -.
DR   KEGG; mtc:MT1831; -.
DR   PATRIC; fig|83331.31.peg.1972; -.
DR   HOGENOM; CLU_022072_1_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
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: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   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Glycosyltransferase; Transferase.
FT   CHAIN           1..724
FT                   /note="4-alpha-glucanotransferase"
FT                   /id="PRO_0000427729"
SQ   SEQUENCE   724 AA;  79745 MW;  153B04525DE738EA CRC64;
     MTELAPSLVE LARRFGIATE YTDWTGRQVL VSEATLVAAL AALGVPAQTE QQRNDALAAQ
     LRSYWARPLP ATIVMRAGEQ TQFRVHVTDG APADVWLQLE DGTTRAEVVQ VDNFTPPFDL
     DGRWIGEASF VLPADLPLGY HRVNLRSGDS QASAAVVVTP DWLGLPDKLA GRRAWGLAVQ
     LYSVRSRQSW GIGDLTDLAN LALWSASAHG AGYVLVNPLH AATLPGPAGR SKPIEPSPYL
     PTSRRFVNPL YLRVEAIPEL VDLPKRGRVQ RLRTNVQQHA DQLDTIDRDS AWAAKRAALK
     LVHRVPRSAG RELAYAAFRT REGRALDDFA TWCALAETYG DDWHRWPKSL RHPDASGVAD
     FVDKHADAVD FHRWLQWQLD EQLASAQSQA LRAGMSLGIM ADLAVGVHPN GADAWALQDV
     LAQGVTAGAP PDEFNQLGQD WSQPPWRPDR LAEQEYRPFR ALIQAALRHA GAVRIDHIIG
     LFRLWWIPDG APPTQGTYVR YDHDAMIGIV ALEAHRAGAV VVGEDLGTVE PWVRDYLLLR
     GLLGTSILWF EQDRDCGPAG TPLPAERWRE YCLSSVTTHD LPPTAGYLAG DQVRLRESLG
     LLTNPVEAEL ESARADRAAW MAELRRVGLL ADGAEPDSEE AVLALYRYLG RTPSRLLAVA
     LTDAVGDRRT QNQPGTTDEY PNWRVPLTGP DGQPMLLEDI FTDRRAATLA EAVRAATTSP
     MSCW