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 27-MAR-2024, entry version 119. 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; Chlamydiota; Chlamydiia; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 KEGG; cca:CCA_00456; -. DR eggNOG; COG1640; Bacteria. DR HOGENOM; CLU_014132_2_1_0; -. DR OrthoDB; 9811841at2; -. 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 Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR003385; Glyco_hydro_77. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR32518; -; 1. DR PANTHER; PTHR32518:SF3; 4-ALPHA-GLUCANOTRANSFERASE; 1. DR Pfam; PF02446; Glyco_hydro_77; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 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 //