ID MALQ_SYNY3 Reviewed; 505 AA. AC P72785; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 19-JAN-2010, entry version 58. 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=sll1676; OS Synechocystis sp. (strain PCC 6803). OC Bacteria; Cyanobacteria; Chroococcales; Synechocystis. OX NCBI_TaxID=1148; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=97061201; PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., RA Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., RA Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., RA Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the RT entire genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). CC -!- CATALYTIC ACTIVITY: Transfers a segment of a (1->4)-alpha-D-glucan CC to a new position in an acceptor, which may be glucose or a CC (1->4)-alpha-D-glucan. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the disproportionating enzyme family. 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; BA000022; BAA16800.1; -; Genomic_DNA. DR PIR; S74648; S74648. DR RefSeq; NP_440120.1; -. DR SMR; P72785; 1-499. DR IntAct; P72785; 1. DR STRING; P72785; -. DR CAZy; GH77; Glycoside Hydrolase Family 77. DR GeneID; 953419; -. DR GenomeReviews; BA000022_GR; sll1676. DR KEGG; syn:sll1676; -. DR NMPDR; fig|1148.1.peg.221; -. DR eggNOG; COG1640; -. DR HOGENOM; HBG704085; -. DR OMA; LQFAFDG; -. DR BioCyc; SSP1148:SLL1676-MONOMER; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004134; F:4-alpha-glucanotransferase activity; IEA:EC. DR GO; GO:0043169; F:cation binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR InterPro; IPR003385; Glyco_hydro_77. DR InterPro; IPR017853; Glyco_hydro_catalytic_core. DR InterPro; IPR013781; Glyco_hydro_sg_catalytic. DR Gene3D; G3DSA:3.20.20.80; Glyco_hydro_cat; 1. DR Pfam; PF02446; Glyco_hydro_77; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Cytoplasm; KW Glycosyltransferase; Transferase. FT CHAIN 1 505 4-alpha-glucanotransferase. FT /FTId=PRO_0000170131. SQ SEQUENCE 505 AA; 57180 MW; 488623C9FA4C9D59 CRC64; MLDKRCSGIL LHPTSLPSRF GIGDLGDGAF QFIDFLADAD QSVWQILPLG PTGFGNSPYL CYSALAINPW LISLDRLAEE GFLPPSLLDQ APPFTNPRVD YDQAIAYKSQ VLKQAFAQFR TNIELAIEQE FAEFCQAQSD WLADYALFMA IKEAHNGAGW HQWDKDIAWR EPEALKIWGD RLKTEVLYHQ FLQFLGFRQW QEVKAYANQR HIAIFGDLPI YVAHDSADVW ANPENFCLDP ETGEAAMMAG VPPDYFSATG QLWGNPVYDW ETLKATGFAW WIKRFKANLQ YLDIVRIDHF RGFESYWGVP QGEKTAENGE WYPAPGKEFF QALGKALGDN LPIVAEDLGV ITPEVEALRD EFNFPGMKVL HFAFDSDRGN PFLPFNYSNG NAVVYTGTHD NDTTVGWFQE RSEDDQQKVI NYLGCVCNEG IHWSLIRLAS SSVAALAIFP LQDILGLGSD CRMNLPGTAA GNWGWRYHPD QLNDWLSGHL SFITELYGRR IYHTD //