ID   MALQ_CHLCV              Reviewed;         530 AA.
AC   O34022;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=CCA_00456;
OS   Chlamydia caviae (strain ATCC VR-813 / DSM 19441 / 03DC25 / GPIC)
OS   (Chlamydophila caviae).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=227941;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC VR-813 / DSM 19441 / 03DC25 / GPIC;
RX   PubMed=9282747; DOI=10.1046/j.1365-2958.1997.4701834.x;
RA   Hsia R.-C., Pannekoek Y., Ingerowski E., Bavoil P.M.;
RT   "Type III secretion genes identify a putative virulence locus of
RT   Chlamydia.";
RL   Mol. Microbiol. 25:351-359(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-813 / DSM 19441 / 03DC25 / GPIC;
RX   PubMed=12682364; DOI=10.1093/nar/gkg321;
RA   Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T.,
RA   Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A.,
RA   Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O.,
RA   Salzberg S.L., Hsia R.-C., McClarty G., Rank R.G., Bavoil P.M.,
RA   Fraser C.M.;
RT   "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC):
RT   examining the role of niche-specific genes in the evolution of the
RT   Chlamydiaceae.";
RL   Nucleic Acids Res. 31:2134-2147(2003).
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; U88070; AAB71512.1; -; Genomic_DNA.
DR   EMBL; AE015925; AAP05202.1; -; Genomic_DNA.
DR   RefSeq; WP_011006418.1; NC_003361.3.
DR   AlphaFoldDB; O34022; -.
DR   SMR; O34022; -.
DR   STRING; 227941.CCA_00456; -.
DR   CAZy; GH77; Glycoside Hydrolase Family 77.
DR   EnsemblBacteria; AAP05202; AAP05202; CCA_00456.
DR   KEGG; cca:CCA_00456; -.
DR   eggNOG; COG1640; Bacteria.
DR   HOGENOM; CLU_014132_2_1_0; -.
DR   OMA; TGQLWGT; -.
DR   OrthoDB; 814704at2; -.
DR   Proteomes; UP000002193; 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..530
FT                   /note="4-alpha-glucanotransferase"
FT                   /id="PRO_0000170122"
SQ   SEQUENCE   530 AA;  61326 MW;  F1D88F6ADD971824 CRC64;
     MTPFSKALRC IQNSPAKQSW KTLGIMPKHG ICLPLFSLHT RNSCGIGEFL DLIPMISWCR
     KHGFQIIQIL PINDSGEDSS PYNSISSVAL NPLYLSLASL PHAQSVAYAN AKLRTMQQLS
     KLPYVHYPQV KAAKWEFLRD YYQYVVKIGA LKDEDFEIFC EKEKYWLRPY TVFRSIKYHL
     KGAPVNNWPK AYTDIKNFTE FEKQFQDECS FFSYLQYLCF QQMSQVKAFA DDNHVFLKGD
     LPILISKDSC DVWYYRQFFS SSGSAGAPPD IYNTEGQNWH LPIYNMHNLV QDNYTWWKAR
     LRYAENFYSL YRLDHIVGLF RLWVWDTSGN GKFQPDDPKE YLPQGTDILT QILRASRMLP
     IGEDLGSVPT DVKETLVKLG ICGTRIPRWE RNWEGDGNFI PLGEYSPLSV TSLSTHDSDT
     LALWWRHAPK EAQKFAQFLG MFFTPVLAEE DQKHILTLSH KTSSIFHINL INDYLALCPD
     LVSNNLKYER INMPGTVSKN NWVYRIKPSV EEILTHDAFN ANIADIFSKI