ID   MALQ_CHLMU              Reviewed;         527 AA.
AC   Q9PKU9;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=TC_0362;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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; AE002160; AAF39223.1; -; Genomic_DNA.
DR   PIR; A81712; A81712.
DR   RefSeq; WP_010230247.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PKU9; -.
DR   SMR; Q9PKU9; -.
DR   STRING; 243161.TC_0362; -.
DR   CAZy; GH77; Glycoside Hydrolase Family 77.
DR   PRIDE; Q9PKU9; -.
DR   EnsemblBacteria; AAF39223; AAF39223; TC_0362.
DR   GeneID; 1245715; -.
DR   KEGG; cmu:TC_0362; -.
DR   eggNOG; COG1640; Bacteria.
DR   HOGENOM; CLU_014132_2_1_0; -.
DR   OMA; TGQLWGT; -.
DR   OrthoDB; 814704at2; -.
DR   Proteomes; UP000000800; 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   Pfam; PF02446; Glyco_hydro_77; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Glycosyltransferase; Transferase.
FT   CHAIN           1..527
FT                   /note="4-alpha-glucanotransferase"
FT                   /id="PRO_0000170120"
SQ   SEQUENCE   527 AA;  61329 MW;  1012A9B5D4309E2A CRC64;
     MPLLSRSLRI IQNSPIRKVW NQVDTSPKHG ICVPLFSIHT QNSCGIGEFL DLIPMIDWCT
     LCGFQILQIL PINDTGSCSS PYNSISSISL NPLHLSISAL PYKEEVSSSR KLIQEMQRLS
     QLSQVNYEKV IPMKRAFFKE YFRVCKSKNL TNHPDFCDFC EREKYWLHPY ALFCSIREHL
     NYLPINHWST TYTDLSYISQ HEHTFAKDIE FYSYLQYLCF EQMKQVRKHA DHKGCLIKGD
     IPILISKDSC DVWFYRKYFS SSESVGSPPD FYNAEGQNWN LPIYNMKTLR QDAYHWWKER
     LRYAENFYSL YRLDHVVGLF RFWVWDELGR GRFEPQDPKD YLDQGTDILS HLLKASSMLP
     IGEDLGTIPV DVKQALESLA VCGTRIPRWE RDWEGTGAYI PFDQYNPLSV TSLSTHDSST
     LALWWQEAPQ EARLFAQFLG MPYTPSLSFH NHKEILKLSH KTSSIFHINL INDYLALCPD
     LISTNPLQER INLPGTISKN NWVYRVKPSI EQLSAHSKLN SLLASLF