ID   MALQ_CHLTR              Reviewed;         527 AA.
AC   O84089;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=CT_087;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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; AE001273; AAC67678.1; -; Genomic_DNA.
DR   PIR; G71557; G71557.
DR   RefSeq; NP_219590.1; NC_000117.1.
DR   RefSeq; WP_010725041.1; NC_000117.1.
DR   AlphaFoldDB; O84089; -.
DR   SMR; O84089; -.
DR   STRING; 813.O172_00470; -.
DR   CAZy; GH77; Glycoside Hydrolase Family 77.
DR   EnsemblBacteria; AAC67678; AAC67678; CT_087.
DR   GeneID; 884150; -.
DR   KEGG; ctr:CT_087; -.
DR   PATRIC; fig|272561.5.peg.95; -.
DR   HOGENOM; CLU_014132_2_1_0; -.
DR   InParanoid; O84089; -.
DR   OMA; TGQLWGT; -.
DR   Proteomes; UP000000431; 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;
KW   Reference proteome; Transferase.
FT   CHAIN           1..527
FT                   /note="4-alpha-glucanotransferase"
FT                   /id="PRO_0000170123"
SQ   SEQUENCE   527 AA;  61454 MW;  52455D5E9ED2D46D CRC64;
     MPSLSQSRRI IQQSSIRKIW NQIDTSPKHG VCVPLFSLYT QESCGIGEFL DLIPMIDWCI
     SCGFQILQIL PINDTGSCSS PYNSISSIAL NPLHLSISAL PYKEEVPAAE TRIREMQQLS
     QLPQVHYEKV RSMKRDFFQE YYRVCKQKKL TDHPDFYAFC EQEKYWLHPY ALFRSIREHL
     DNLPINHWPT TYTDLSQITE HERTFAEDIQ FHSYLQYLCF QQMTQVREHA NCKSCLIKGD
     IPILISKDSC DVWFYRHYFS SSESVGAPPD LYNAEGQNWH LPICNMKTLQ QDNYLWWKER
     LRYAENFYSL YRLDHVVGLF RFWVWDESGC GRFEPHDPKN YLAQGQDILS HLLTSSSMLP
     IGEDLGTIPS DVKRMLESFA VCGTRIPRWE RNWEGNGAYT PFDQYDPLSV TSLSTHDSST
     LASWWKESPQ ESKLFAQFLG LPYSSTLSLH NHTEILKLSH KTSSIFRINL INDYLALFPD
     LISKTPRYER INLPGTISKN NWVYRVKPSI EDLSSHSKLN SLLEALF