ID   MALQ_MYCBO              Reviewed;         724 AA.
AC   P65337; A0A1R3Y047; O53932; X2BIU5;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=BQ2027_MB1810C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIU00414.1; -; Genomic_DNA.
DR   RefSeq; NP_855463.1; NC_002945.3.
DR   RefSeq; WP_003408795.1; NC_002945.4.
DR   AlphaFoldDB; P65337; -.
DR   SMR; P65337; -.
DR   EnsemblBacteria; SIU00414; SIU00414; BQ2027_MB1810C.
DR   GeneID; 45425759; -.
DR   PATRIC; fig|233413.5.peg.1989; -.
DR   OMA; QYPNWRL; -.
DR   Proteomes; UP000001419; 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_0000170128"
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